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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 Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:12051944
ChainResidueDetails
AGLU402

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: in inhibited form => ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439
ChainResidueDetails
ACYS99

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051944
ChainResidueDetails
AASP131
AASP205
AASP206
AGLU208
AASP165
AASP182
AGLY183
AASP185
ALEU187
AGLY197
AGLN199
AASP201

site_idSWS_FT_FI4
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439
ChainResidueDetails
AHIS175
AASP177
AHIS190
AHIS203
AHIS401
AHIS405
AHIS411

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Cleavage; by MMP3 => ECO:0000269|PubMed:1371271
ChainResidueDetails
AGLU59
AARG106

site_idSWS_FT_FI6
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN38
AASN120
AASN127

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

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PDB entries from 2024-07-24

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