EzCatDB: D00173

DB codeD00173
CATH domainDomain 1-.-.-.-
Domain 22.120.10.10Catalytic domain
E.C.3.2.1.18
CSA1a4g,7nn9

CATH domainRelated DB codes (homologues)
2.120.10.10M00310,T00064,T00065,T00208

Enzyme Name
Swiss-protKEGG

P03472P05803P27907
Protein nameNeuraminidaseNeuraminidaseNeuraminidaseexo-alpha-sialidase
neuraminidase
sialidase
alpha-neuraminidase
acetylneuraminidase
SynonymsEC 3.2.1.18
EC 3.2.1.18
EC 3.2.1.18

KEGG pathways
MAP codePathways
MAP00511N-Glycan degradation
MAP00600Sphingolipid metabolism
MAP01032Glycan structures - degradation

Swiss-prot:Accession NumberP03472P05803P27907
Entry nameNRAM_I75A5NRAM_I84A1NRAM_INBBE
ActivityHydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
SubunitHomotetramer (By similarity).Homotetramer (By similarity).Homotetramer.
Subcellular locationVirion membrane (By similarity). Apical cell membrane, Single-pass type II membrane protein (By similarity). Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane (By similarity).Virion membrane (By similarity). Apical cell membrane, Single-pass type II membrane protein (By similarity). Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane (By similarity).Virion membrane (By similarity). Apical cell membrane, Single-pass type II membrane protein (By similarity). Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. In the virion, forms a mushroom-shaped spike on the surface of the membrane (By similarity).
CofactorBinds 1 calcium ion (By similarity).Binds 1 calcium ion.


SubstratesProductsintermediates
KEGG-idC00001C06128C04730C04884C04927C06139C06140C00270C02686C01290C06135C04911C06140C06141
CompoundH2ON-Acetylneuraminyl-galactosylceramide(N-Acetylneuraminyl)-D-galactosyl-D-glucosylceramideN-Acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramideN-Acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramideNeu5Ac-alpha2->8Neu5Ac-alpha2->3Gal-beta1->3GalNAc-beta1->4(Neu5Ac-alpha2->8Neu5Ac-alpha2->3)Gal-beta1->4Glc-beta1->1'CerNeu5Ac-alpha2->3Gal-beta1->3GalNAc-beta1->4(Neu5Ac-alpha2->8Neu5Ac-alpha2->3)Gal-beta1->4Glc-beta1->1'CerN-AcetylneuraminateGalactosylceramidebeta-D-Galactosyl-1,4-beta-D-glucosylceramideGalNAc-beta1->4Gal-beta1->4Glc-beta1->1'CerD-Galactosyl-N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramideNeu5Ac-alpha2->3Gal-beta1->3GalNAc-beta1->4(Neu5Ac-alpha2->8Neu5Ac-alpha2->3)Gal-beta1->4Glc-beta1->1'CerGal-beta1->3GalNAc-beta1->4(Neu5Ac-alpha2->8Neu5Ac-alpha2->3)Gal-beta1->4Glc-beta1->1'Cer
TypeH2Oamide group,carbohydrate,carboxyl group,lipidamide group,carbohydrate,carboxyl group,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipid,polysaccharideamide group,carbohydrate,carboxyl groupamide group,carbohydrate,lipidamide group,carbohydrate,lipid,polysaccharideamide group,carbohydrate,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipid,polysaccharideamide group,carbohydrate,carboxyl group,lipidamide group,carbohydrate,carboxyl group,lipid,polysaccharide
1a14N
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1f8bA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DAN
1f8cA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:4AM
1f8dA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:9AM
1f8eA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:49A
1inyA
UnboundUnboundUnboundUnboundUnboundUnboundAnalogue:EQPUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1l7fA
UnboundUnboundUnboundUnboundUnboundUnboundAnalogue:BCZUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1l7gA
UnboundUnboundUnboundUnboundUnboundUnboundAnalogue:BCZUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1l7hA
UnboundUnboundUnboundUnboundUnboundUnboundAnalogue:BCZUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1mweA
UnboundUnboundUnboundUnboundUnboundUnboundBound:SIA 1UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ncaN
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ncbN
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1nccN
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1nmcA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1nmcN
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1nnaA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1nnbA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DAN
1nncA
UnboundUnboundUnboundUnboundUnboundUnboundAnalogue:ZMRUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2qwaA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2qwbA
UnboundUnboundUnboundUnboundUnboundUnboundBound:SIA 800UnboundUnboundUnboundUnboundUnboundUnboundUnbound
2qwcA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DAN
2qwdA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:4AM
2qweA
UnboundUnboundUnboundUnboundUnboundUnboundAnalogue:GNAUnboundUnboundUnboundUnboundUnboundUnboundUnbound
2qwfA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:G20
2qwgA
UnboundUnboundUnboundUnboundUnboundUnboundAnalogue:G28UnboundUnboundUnboundUnboundUnboundUnboundUnbound
2qwhA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:G39
2qwiA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:G20
2qwjA
UnboundUnboundUnboundUnboundUnboundUnboundAnalogue:G28UnboundUnboundUnboundUnboundUnboundUnboundUnbound
2qwkA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:G39
3nn9A
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
4nn9A
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
5nn9A
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
6nn9A
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
7nn9A
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ncdN
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1nmaN
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1nmbN
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1a4gA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:ZMR
1a4gB
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:ZMR
1a4qA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DPC
1a4qB
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DPC
1nsbA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1nsbB
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1nscA
UnboundUnboundUnboundUnboundUnboundUnboundBound:SIAUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1nscB
UnboundUnboundUnboundUnboundUnboundUnboundBound:SIAUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1nsdA
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DAN
1nsdB
UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:DAN

Active-site residues
resource
Literature [9]
pdbCatalytic residuescomment
1a14NASP 151;GLU 277;TYR 406

1f8bAASP 151;GLU 277;TYR 406

1f8cAASP 151;GLU 277;TYR 406

1f8dAASP 151;GLU 277;TYR 406

1f8eAASP 151;GLU 277;TYR 406

1inyAASP 151;GLU 278;TYR 405

1l7fAASP 151;GLU 277;TYR 406

1l7gAASP 151;GLU 277;TYR 406
mutant E119G
1l7hAASP 151;GLU 277;TYR 406
mutant R292K
1mweAASP 151;GLU 277;TYR 406

1ncaNASP 151;GLU 277;TYR 406

1ncbNASP 151;GLU 277;TYR 406
mutant N329D
1nccNASP 151;GLU 277;TYR 406
mutant I368R
1nmcAASP 151;GLU 277;TYR 406

1nmcNASP 151;GLU 277;TYR 406

1nnaAASP 152;GLU 279;TYR 406

1nnbAASP 152;GLU 279;TYR 406

1nncAASP 151;GLU 277;TYR 406

2qwaAASP 151;GLU 277;TYR 406
mutant R292K
2qwbAASP 151;GLU 277;TYR 406
mutant R292K
2qwcAASP 151;GLU 277;TYR 406
mutant R292K
2qwdAASP 151;GLU 277;TYR 406
mutant R292K
2qweAASP 151;GLU 277;TYR 406
mutant R292K
2qwfAASP 151;GLU 277;TYR 406
mutant R292K
2qwgAASP 151;GLU 277;TYR 406
mutant R292K
2qwhAASP 151;GLU 277;TYR 406
mutant R292K
2qwiAASP 151;GLU 277;TYR 406

2qwjAASP 151;GLU 277;TYR 406
mutant R292K
2qwkAASP 151;GLU 277;TYR 406

3nn9AASP 151;GLU 277;TYR 406
mutant N329D
4nn9AASP 151;GLU 277;TYR 406
mutant I368R
5nn9AASP 151;GLU 277;TYR 406
mutant A369D
6nn9AASP 151;GLU 277;TYR 406
mutant K432N
7nn9AASP 151;GLU 277;TYR 406

1ncdNASP 151;GLU 277;TYR 406

1nmaNASP 151;GLU 277;TYR 406

1nmbNASP 151;GLU 277;TYR 406

1a4gAASP 148;GLU 275;TYR 408

1a4gBASP 148;GLU 275;TYR 408

1a4qAASP 148;GLU 275;TYR 408

1a4qBASP 148;GLU 275;TYR 408

1nsbAASP 148;GLU 275;TYR 408

1nsbBASP 148;GLU 275;TYR 408

1nscAASP 148;GLU 275;TYR 408

1nscBASP 148;GLU 275;TYR 408

1nsdAASP 148;GLU 275;TYR 408

1nsdBASP 148;GLU 275;TYR 408


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[12]


references
[1]
PubMed ID3811232
JournalVirology
Year1987
Volume156
Pages181-4
AuthorsLaver WG, Webster RG, Colman PM
TitleCrystals of antibodies complexed with influenza virus neuraminidase show isosteric binding of antibody to wild-type and variant antigens.
[2]
PubMed ID2569208
JournalPhilos Trans R Soc Lond B Biol Sci
Year1989
Volume323
Pages511-8
AuthorsColman PM, Tulip WR, Varghese JN, Tulloch PA, Baker AT, Laver WG, Air GM, Webster RG
TitleThree-dimensional structures of influenza virus neuraminidase-antibody complexes.
[3]
PubMed ID1700825
JournalJ Virol
Year1990
Volume64
Pages5797-803
AuthorsAir GM, Laver WG, Webster RG
TitleMechanism of antigenic variation in an individual epitope on influenza virus N9 neuraminidase.
[4]
PubMed ID1866839
JournalUltramicroscopy
Year1991
Volume35
Pages131-43
AuthorsBullough PA, Tulloch PA
TitleSpot-scan imaging of microcrystals of an influenza neuraminidase-antibody fragment complex.
[5]
PubMed ID1920429
JournalJ Mol Biol
Year1991
Volume221
Pages487-97
AuthorsTulip WR, Varghese JN, Baker AT, van Donkelaar A, Laver WG, Webster RG, Colman PM
TitleRefined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants.
Related PDB3nn9,4nn9,5nn9,6nn9
[6]
PubMed ID1984652
JournalVirology
Year1991
Volume180
Pages266-72
AuthorsBurmeister WP, Daniels RS, Dayan S, Gagnon J, Cusack S, Ruigrok RW
TitleSequence and crystallization of influenza virus B/Beijing/1/87 neuraminidase.
Related PDB1nsb
[7]
CommentsX-ray crystallography
PubMed ID1381757
JournalJ Mol Biol
Year1992
Volume227
Pages122-48
AuthorsTulip WR, Varghese JN, Laver WG, Webster RG, Colman PM
TitleRefined crystal structure of the influenza virus N9 neuraminidase-NC41 Fab complex.
Related PDB1nca
[8]
CommentsX-ray crystallography
PubMed ID1522584
JournalJ Mol Biol
Year1992
Volume227
Pages149-59
AuthorsTulip WR, Varghese JN, Webster RG, Laver WG, Colman PM
TitleCrystal structures of two mutant neuraminidase-antibody complexes with amino acid substitutions in the interface.
Related PDB1ncb,1ncc,1ncd
[9]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 83-470.
Medline ID93381688
PubMed ID8371267
JournalJ Mol Biol
Year1993
Volume232
Pages1069-83
AuthorsBossart-Whitaker P, Carson M, Babu YS, Smith CD, Laver WG, Air GM
TitleThree-dimensional structure of influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy 2,3-dehydro-N-acetyl neuraminic acid.
Related PDB1nna,1nnb
Related Swiss-protP03472
[10]
PubMed ID8497484
JournalProteins
Year1993
Volume16
Pages57-63
AuthorsMalby RL, Caldwell JB, Gruen LC, Harley VR, Ivancic N, Kortt AA, Lilley GG, Power BE, Webster RG, Colman PM, et al
TitleRecombinant antineuraminidase single chain antibody: expression, characterization, and crystallization in complex with antigen.
[11]
PubMed ID7680132
JournalProteins
Year1993
Volume15
Pages121-32
AuthorsNuss JM, Whitaker PB, Air GM
TitleIdentification of critical contact residues in the NC41 epitope of a subtype N9 influenza virus neuraminidase.
[12]
PubMed ID8069621
JournalStructure
Year1993
Volume1
Pages19-26
AuthorsBurmeister WP, Henrissat B, Bosso C, Cusack S, Ruigrok RW
TitleInfluenza B virus neuraminidase can synthesize its own inhibitor.
Related PDB1nsc,1nsd
[13]
CommentsX-ray crystallography
PubMed ID7517697
JournalBiochemistry
Year1994
Volume33
Pages7986-97
AuthorsTulip WR, Harley VR, Webster RG, Novotny J
TitleN9 neuraminidase complexes with antibodies NC41 and NC10: empirical free energy calculations capture specificity trends observed with mutant binding data.
Related PDB1nma
[14]
PubMed ID8168505
JournalEur J Biochem
Year1994
Volume221
Pages151-7
AuthorsKortt AA, Malby RL, Caldwell JB, Gruen LC, Ivancic N, Lawrence MC, Howlett GJ, Webster RG, Hudson PJ, Colman PM
TitleRecombinant anti-sialidase single-chain variable fragment antibody. Characterization, formation of dimer and higher-molecular-mass multimers and the solution of the crystal structure of the single-chain variable fragment/sialidase complex.
[15]
PubMed ID7507170
JournalJ Mol Biol
Year1994
Volume235
Pages747-59
AuthorsNuss JM, Air GM
TitleDefining the requirements for an antibody epitope on influenza virus neuraminidase: how tolerant are protein epitopes?
[16]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID95086861
PubMed ID7994573
JournalStructure
Year1994
Volume2
Pages733-46
AuthorsMalby RL, Tulip WR, Harley VR, McKimm-Breschkin JL, Laver WG, Webster RG, Colman PM
TitleThe structure of a complex between the NC10 antibody and influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody.
Related PDB1nmb
Related Swiss-protP05803
[17]
PubMed ID7576085
JournalJ Protein Chem
Year1995
Volume14
Pages167-78
AuthorsKortt AA, Guthrie RE, Hinds MG, Power BE, Ivancic N, Caldwell JB, Gruen LC, Norton RS, Hudson PJ
TitleSolution properties of Escherichia coli-expressed VH domain of anti-neuraminidase antibody NC41.
[18]
PubMed ID7549872
JournalProtein Sci
Year1995
Volume4
Pages1081-7
AuthorsVarghese JN, Epa VC, Colman PM
TitleThree-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase.
Related PDB1nnc,7nn9
[19]
PubMed ID7844831
JournalJ Mol Biol
Year1995
Volume245
Pages623-34
AuthorsWhite CL, Janakiraman MN, Laver WG, Philippon C, Vasella A, Air GM, Luo M
TitleA sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies.
Related PDB1iny
[20]
PubMed ID8535779
JournalStructure
Year1995
Volume3
Pages853-9
AuthorsDavies G, Henrissat B
TitleStructures and mechanisms of glycosyl hydrolases.
[21]
PubMed ID8552677
JournalProc Natl Acad Sci U S A
Year1996
Volume93
Pages7-12
AuthorsDavies DR, Cohen GH
TitleInteractions of protein antigens with antibodies.
[22]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 83-470.
Medline ID98004480
PubMed ID9342319
JournalProc Natl Acad Sci U S A
Year1997
Volume94
Pages11808-12
AuthorsVarghese JN, Colman PM, van Donkelaar A, Blick TJ, Sahasrabudhe A, McKimm-Breschkin JL
TitleStructural evidence for a second sialic acid binding site in avian influenza virus neuraminidases.
Related PDB1mwe
Related Swiss-protP03472
[23]
PubMed ID9194168
JournalProtein Eng
Year1997
Volume10
Pages423-33
AuthorsKortt AA, Lah M, Oddie GW, Gruen CL, Burns JE, Pearce LA, Atwell JL, McCoy AJ, Howlett GJ, Metzger DW, Webster RG, Hudson PJ
TitleSingle-chain Fv fragments of anti-neuraminidase antibody NC10 containing five- and ten-residue linkers form dimers and with zero-residue linker a trimer.
[24]
CommentsX-ray crystallography
PubMed ID9642070
JournalJ Mol Biol
Year1998
Volume279
Pages901-10
AuthorsMalby RL, McCoy AJ, Kortt AA, Hudson PJ, Colman PM
TitleThree-dimensional structures of single-chain Fv-neuraminidase complexes.
Related PDB1a14,1nmc
[25]
PubMed ID9655825
JournalStructure
Year1998
Volume6
Pages735-46
AuthorsVarghese JN, Smith PW, Sollis SL, Blick TJ, Sahasrabudhe A, McKimm-Breschkin JL, Colman PM
TitleDrug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase.
Related PDB2qwa,2qwb,2qwc,2qwd,2qwe,2qwe,2qwf,2qwg,2qwh,2qwi,2qwj,2qwk
[26]
PubMed ID9526556
JournalJ Med Chem
Year1998
Volume41
Pages798-807
AuthorsTaylor NR, Cleasby A, Singh O, Skarzynski T, Wonacott AJ, Smith PW, Sollis SL, Howes PD, Cherry PC, Bethell R, Colman P, Varghese J
TitleDihydropyrancarboxamides related to zanamivir: a new series of inhibitors of influenza virus sialidases. 2. Crystallographic and molecular modeling study of complexes of 4-amino-4H-pyran-6-carboxamides and sialidase from influenza virus types A and B.
Related PDB1a4g,1a4q
[27]
PubMed ID11274459
JournalProtein Sci
Year2001
Volume10
Pages689-96
AuthorsSmith BJ, Colman PM, Von Itzstein M, Danylec B, Varghese JN
TitleAnalysis of inhibitor binding in influenza virus neuraminidase.
Related PDB1f8b,1f8c,1f8d,1f8e
[28]
PubMed ID12014958
JournalJ Med Chem
Year2002
Volume45
Pages2207-12
AuthorsSmith BJ, McKimm-Breshkin JL, McDonald M, Fernley RT, Varghese JN, Colman PM
TitleStructural studies of the resistance of influenza virus neuramindase to inhibitors.
Related PDB1l7f,1l7g,1l7h
[29]
PubMed ID12054776
JournalJ Mol Biol
Year2002
Volume318
Pages161-77
AuthorsSheinerman FB, Honig B
TitleOn the role of electrostatic interactions in the design of protein-protein interfaces.

comments
This enzyme belongs to the glycosidase family-34. This enzyme is a retaining glycosidase enzyme.
According to literature [9], mutations at conserved residues, Glu277 and Tyr406 (of 1a14), inactivated the enzyme, which suggested that they can be involved in catalysis.
Another paper [12] reported that Tyr406 might stabilize the transition state during catalysis. Acording to the paper, the catalytic mechanism of this enzyme is distinct from that of other glycosidase enzymes.

createdupdated
2004-05-292009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

© Computational Biology Research Center, AIST, 2004 All Rights Reserved.