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1PEX

COLLAGENASE-3 (MMP-13) C-TERMINAL HEMOPEXIN-LIKE DOMAIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0030574biological_processcollagen catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 500
ChainResidue
AASN326
AARG327
AARG344
AARG346

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 501
ChainResidue
AILE287
AALA331
AALA380
AVAL429
ACA503

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 502
ChainResidue
AASP285
AASP329
ASER378
AASP427

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 503
ChainResidue
AILE287
AALA331
AALA380
AVAL429
ACL501
ACL504

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 504
ChainResidue
ACA503

Functional Information from PROSITE/UniProt
site_idPS00024
Number of Residues16
DetailsHEMOPEXIN Hemopexin domain signature. TKsfWpelPnRIDAAY
ChainResidueDetails
ATHR317-TYR332

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305
ChainResidueDetails
AASP285
AILE287
AASP329
AALA331
ASER378
AALA380
AASP427
AVAL429

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by PKDCC => ECO:0000303|PubMed:25171405
ChainResidueDetails
ATYR360

219140

PDB entries from 2024-05-01

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