EzCatDB: M00101

DB codeM00101
CATH domainDomain 13.40.390.10Catalytic domain
Domain 22.10.10.10
Domain 32.10.10.10
Domain 42.10.10.10
Domain 52.110.10.10
E.C.3.4.24.24
CSA1ck7,1qib

CATH domainRelated DB codes (homologues)
2.110.10.10D00232
3.40.390.10S00394,S00395,S00397,S00398,S00399,D00232,D00236

Enzyme Name
Swiss-protKEGG

P08253
Protein name72 kDa type IV collagenasegelatinase A
72-kDa gelatinase
matrix metalloproteinase 2
type IV collagenase
3/4 collagenase (Obsolete)
matrix metalloproteinase 5 (Obsolete)
72 kDa gelatinase type A
collagenase IV
collagenase type IV
MMP 2
type IV collagen metalloproteinase
type IV collagenase/gelatinase
matrix metalloproteinase 2
SynonymsEC 3.4.24.24
72 kDa gelatinase
Matrix metalloproteinase-2
MMP-2
Gelatinase A
TBE-1


Swiss-prot:Accession NumberP08253
Entry nameMMP2_HUMAN
ActivityCleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|- Ile-Ala-Gly-Gln.
SubunitLigand for integrin alpha-V/beta-3.
Subcellular locationSecreted, extracellular space, extracellular matrix (Probable).
CofactorBinds 4 calcium ions per subunit.,Binds 2 zinc ions per subunit.


CofactorsSubstratesProducts
KEGG-idC00038C00076C00560C00335C00421C02531C02259C00001C00017C00012
CompoundZincCalciumGelatin type ICollagen type IVCollagen type VCollagen type VIICollagen type XH2OProteinPeptide
Typeheavy metaldivalent metal (Ca2+, Mg2+)peptide/proteinpeptide/proteinpeptide/proteinpeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein
1ck7A01Bound:2x_ZNBound:2x_CAUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1qibABound:2x_ZNBound:3x_CAUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1gxdA01Bound:2x_ZNBound:_CAUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1gxdB01Bound:2x_ZNBound:_CAUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakA01Bound:2x_ZNBound:2x_CAUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakB01Bound:2x_ZNBound:2x_CAUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakC01Bound:2x_ZNBound:2x_CAUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakD01Bound:2x_ZNBound:2x_CAUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1ck7A02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1gxdA02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1gxdB02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakA02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundAnalogue:GLY-PRO-ALA-GLY-PRO-PRO-GLY-ALA
1eakB02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakC02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakD02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundAnalogue:GLY-PRO-ALA-GLY-PRO-PRO-GLY-ALA
1ck7A03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1gxdA03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1gxdB03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakA03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakB03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakC03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakD03UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1cxwAUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1ck7A04UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1gxdA04UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1gxdB04UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakA04UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakB04UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakC04UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1eakD04UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1j7mAUnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1ck7A05UnboundBound:_CAUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1gxdA05UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1gxdB05UnboundUnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound

Active-site residues
pdbCatalytic residuesCofactor-binding residuescomment
1ck7A01       
CYS 102;HIS 403;HIS 407;HIS 413(catalytic Zinc)
mutant E404A
1qibAGLU 202
       ;HIS 201;HIS 205;HIS 211(catalytic Zinc)

1gxdA01       
CYS  73;HIS 374;HIS 378;HIS 384(catalytic Zinc)
mutant E375A
1gxdB01       
CYS  73;HIS 374;HIS 378;HIS 384(catalytic Zinc)
mutant E375A
1eakA01       
CYS 102;HIS 403;HIS 407;HIS 413(catalytic Zinc)
mutant E404Q
1eakB01       
CYS 102;HIS 403;HIS 407;HIS 413(catalytic Zinc)
mutant E404Q
1eakC01       
CYS 102;HIS 403;HIS 407;HIS 413(catalytic Zinc)
mutant E404Q
1eakD01       
CYS 102;HIS 403;HIS 407;HIS 413(catalytic Zinc)
mutant E404Q
1ck7A02


1gxdA02


1gxdB02


1eakA02


1eakB02


1eakC02


1eakD02


1ck7A03


1gxdA03


1gxdB03


1eakA03


1eakB03


1eakC03


1eakD03


1cxwA


1ck7A04


1gxdA04


1gxdB04


1eakA04


1eakB04


1eakC04


1eakD04


1j7mA


1ck7A05


1gxdA05


1gxdB05



References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]p.1667-1669

references
[1]
PubMed ID7583664
JournalNat Struct Biol
Year1995
Volume2
Pages938-42
AuthorsLibson AM, Gittis AG, Collier IE, Marmer BL, Goldberg GI, Lattman EE
TitleCrystal structure of the haemopexin-like C-terminal domain of gelatinase A.
[2]
PubMed ID8549817
JournalFEBS Lett
Year1996
Volume378
Pages126-30
AuthorsGohlke U, Gomis-Ruth FX, Crabbe T, Murphy G, Docherty AJ, Bode W
TitleThe C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function.
[3]
JournalCroatica Chemica Acta
Year1999
Volume72
Pages575-591
AuthorsDhanaraj V, Williams_MG, Ye_QZ, Molina_F, Johnson_LL, Ortwine_DF, Pavlovsky_A, Rubin_JR, Skeean_RW, White_AD, Humblet_C, Hupe_DJ, Blundell_TL
TitleX-ray structure of gelatinase a catalytic domain complexed with a hydroxamate inhibitor.
Related PDB1qib
[4]
CommentsX-ray crystallography
PubMed ID10356396
JournalScience
Year1999
Volume284
Pages1667-70
AuthorsMorgunova E, Tuuttila A, Bergmann U, Isupov M, Lindqvist Y, Schneider G, Tryggvason K
TitleStructure of human pro-matrix metalloproteinase-2: activation mechanism revealed.
Related PDB1ck7
[5]
PubMed ID10545322
JournalStructure Fold Des
Year1999
Volume7
Pages1235-45
AuthorsBriknarova K, Grishaev A, Banyai L, Tordai H, Patthy L, Llinas M
TitleThe second type II module from human matrix metalloproteinase 2: structure, function and dynamics.
Related PDB1cxw
[6]
PubMed ID11320090
JournalJ Biol Chem
Year2001
Volume276
Pages27613-21
AuthorsBriknarova K, Gehrmann M, Banyai L, Tordai H, Patthy L, Llinas M
TitleGelatin-binding region of human matrix metalloproteinase-2: solution structure, dynamics, and function of the COL-23 two-domain construct.
Related PDB1j7m
[7]
PubMed ID11390386
JournalJ Biol Chem
Year2001
Volume276
Pages32966-70
AuthorsWilliamson RA, Hutton M, Vogt G, Rapti M, Knauper V, Carr MD, Murphy G
TitleTyrosine 36 plays a critical role in the interaction of the AB loop of tissue inhibitor of metalloproteinases-2 with matrix metalloproteinase-14.
[8]
PubMed ID11513874
JournalFEBS Lett
Year2001
Volume503
Pages158-62
AuthorsPatterson ML, Atkinson SJ, Knauper V, Murphy G
TitleSpecific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain.
[9]
PubMed ID11566806
JournalBiophys J
Year2001
Volume81
Pages2370-7
AuthorsCollier IE, Saffarian S, Marmer BL, Elson EL, Goldberg G
TitleSubstrate recognition by gelatinase A: the C-terminal domain facilitates surface diffusion.
[10]
PubMed ID12023034
JournalFEBS Lett
Year2002
Volume519
Pages147-52
AuthorsLee SJ, Jang JW, Kim YM, Lee HI, Jeon JY, Kwon YG, Lee ST
TitleEndostatin binds to the catalytic domain of matrix metalloproteinase-2.
[11]
PubMed ID12032297
JournalProc Natl Acad Sci U S A
Year2002
Volume99
Pages7414-9
AuthorsMorgunova E, Tuuttila A, Bergmann U, Tryggvason K
TitleStructural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.
Related PDB1gxd
[12]
PubMed ID12147339
JournalBiochim Biophys Acta
Year2002
Volume1598
Pages10-23
AuthorsFeng Y, Likos JJ, Zhu L, Woodward H, Munie G, McDonald JJ, Stevens AM, Howard CP, De Crescenzo GA, Welsch D, Shieh HS, Stallings WC
TitleSolution structure and backbone dynamics of the catalytic domain of matrix metalloproteinase-2 complexed with a hydroxamic acid inhibitor.
[13]
PubMed ID12486137
JournalJ Biol Chem
Year2003
Volume278
Pages12241-6
AuthorsTrexler M, Briknarova K, Gehrmann M, Llinas M, Patthy L
TitlePeptide ligands for the fibronectin type II modules of matrix metalloproteinase 2 (MMP-2).
[14]
PubMed ID12642591
JournalJ Biol Chem
Year2003
Volume278
Pages18140-5
AuthorsLauer-Fields JL, Sritharan T, Stack MS, Nagase H, Fields GB
TitleSelective hydrolysis of triple-helical substrates by matrix metalloproteinase-2 and -9.
[15]
PubMed ID12878590
JournalJ Biol Chem
Year2003
Volume278
Pages38765-71
AuthorsJiang A, Pei D
TitleDistinct roles of catalytic and pexin-like domains in membrane-type matrix metalloproteinase (MMP)-mediated pro-MMP-2 activation and collagenolysis.

comments
This enzyme belongs to the peptidase family M10A.
Although the catalytic residue and catalytic zinc are annotated, the detailed catalytic mechanism is still unclear.

createdupdated
2002-08-272009-02-26


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.