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1L6J

Crystal structure of human matrix metalloproteinase MMP9 (gelatinase B).

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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 500
ChainResidue
ACYS99
AHIS401
AHIS405
AHIS411

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
AHIS175
AASP177
AHIS190
AHIS203

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 502
ChainResidue
AGLY183
AGLY186
ALEU187
AASP205
AGLU208
AASP182

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 503
ChainResidue
AASP131
AASP206
AGLU208
AHOH1054

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 504
ChainResidue
AALA164
AASP165
AGLY197
AGLN199
AASP201
AHOH1052
AHOH1174

Functional Information from PROSITE/UniProt
site_idPS00023
Number of Residues42
DetailsFN2_1 Fibronectin type-II collagen-binding domain signature. ChfPFiFegrsysaCttdgrsdglpWCsttaNYdtddrFgFC
ChainResidueDetails
ACYS230-CYS271
ACYS288-CYS329
ACYS347-CYS388

site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHAL
ChainResidueDetails
AVAL398-LEU407

site_idPS00546
Number of Residues8
DetailsCYSTEINE_SWITCH Matrixins cysteine switch. PRCGvPDL
ChainResidueDetails
APRO97-LEU104

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsDomain: {"description":"Fibronectin type-II 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues48
DetailsDomain: {"description":"Fibronectin type-II 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues48
DetailsDomain: {"description":"Fibronectin type-II 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsMotif: {"description":"Cysteine switch","evidences":[{"source":"PubMed","id":"12077439","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"description":"in inhibited form","evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12077439","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12051944","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12077439","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsSite: {"description":"Cleavage; by MMP3","evidences":[{"source":"PubMed","id":"1371271","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
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
AMET419
AGLU402

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AARG221

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU402

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AALA228

246031

PDB entries from 2025-12-10

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