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3DPF

Crystal structure of the complex between MMP-8 and a non-zinc chelating inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 996
ChainResidue
AASP137
AGLY169
AGLY171
AASP173

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 997
ChainResidue
AGLU180
AASP154
AGLY155
AASN157
AILE159
AASP177

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 998
ChainResidue
AHIS147
AASP149
AHIS162
AHIS175

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 999
ChainResidue
AHIS197
AHIS201
AHIS207

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 996
ChainResidue
BASP137
BGLY169
BGLY171
BASP173

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 997
ChainResidue
BASP154
BGLY155
BASN157
BILE159
BASP177
BGLU180

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 998
ChainResidue
BHIS147
BASP149
BHIS162
BHIS175

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 999
ChainResidue
BHIS197
BHIS201
BHIS207

site_idAC9
Number of Residues19
DetailsBINDING SITE FOR RESIDUE AXB A 1
ChainResidue
AILE159
ALEU160
AALA161
ALEU193
AHIS197
AGLU198
AALA213
ALEU214
ATYR216
APRO217
AASN218
ATYR219
AALA220
AARG222
ATHR224
AASN226
ATYR227
ASER228
APRO230

site_idBC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE AXB B 2
ChainResidue
BGLY158
BILE159
BLEU160
BALA161
BLEU193
BHIS197
BGLU198
BALA213
BLEU214
BTYR216
BPRO217
BASN218
BTYR219
BALA220
BARG222
BTHR224
BASN226
BTYR227
BSER228
BPRO230

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HAE A 3
ChainResidue
AILE159
AHIS162

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHSL
ChainResidueDetails
AVAL194-LEU203

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues26
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8137810","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
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
AMET215
AGLU198

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
BMET215
BGLU198

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU198

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
BGLU198

238582

PDB entries from 2025-07-09

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