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1FBL

STRUCTURE OF FULL-LENGTH PORCINE SYNOVIAL COLLAGENASE (MMP1) REVEALS A C-TERMINAL DOMAIN CONTAINING A CALCIUM-LINKED, FOUR-BLADED BETA-PROPELLER

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 993
ChainResidue
AASP124
AGLU199
AGLU201

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 994
ChainResidue
AASP285
AGLN329
AASP378
AASP427

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 995
ChainResidue
AGLY192
AASP194
AHOH834
AHOH837
AASP158
AGLY190

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 996
ChainResidue
AASP175
AGLY176
AGLY178
AASN180
AASP198
AGLU201

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 997
ChainResidue
AHIS168
AASP170
AHIS183
AHIS196

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 998
ChainResidue
AHIS218
AHIS222
AHIS228
AHTA900

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE HTA A 900
ChainResidue
AGLY179
AASN180
ALEU181
AALA182
AHIS218
AGLU219
AHIS222
AHIS228
APRO238
AASN239
ATYR240
AHOH505
AHOH531
AHOH559
AZN998

Functional Information from PROSITE/UniProt
site_idPS00024
Number of Residues16
DetailsHEMOPEXIN Hemopexin domain signature. ISvfWpqvPnGLQAAY
ChainResidueDetails
AILE317-TYR332

site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHELGHSL
ChainResidueDetails
AVAL215-LEU224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues49
DetailsRepeat: {"description":"Hemopexin 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues46
DetailsRepeat: {"description":"Hemopexin 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues48
DetailsRepeat: {"description":"Hemopexin 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues43
DetailsRepeat: {"description":"Hemopexin 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8590015","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues23
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Cleavage; by autolysis"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P03956","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by PKDCC","evidences":[{"source":"UniProtKB","id":"P03956","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AMET236
AGLU219

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU219

246704

PDB entries from 2025-12-24

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