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3DNG

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 Residues15
DetailsBINDING SITE FOR RESIDUE AXA A 1
ChainResidue
APHE192
ALEU193
AHIS197
AALA213
ALEU214
ATYR216
APRO217
AASN218
ATYR219
AALA220
APHE221
AARG222
ATHR224
ATYR227
ASER228

site_idBC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AXA B 2
ChainResidue
BLEU193
BHIS197
BALA213
BLEU214
BTYR216
BPRO217
BASN218
BTYR219
BALA220
BPHE221
BARG222
BTHR224
BTYR227
BSER228

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
DetailsACT_SITE:
ChainResidueDetails
AGLU198
BGLU198

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AASP137
AGLY169
AGLY171
AASP173
BASP137
BGLY169
BGLY171
BASP173

site_idSWS_FT_FI3
Number of Residues26
DetailsBINDING: BINDING => ECO:0000269|PubMed:8137810
ChainResidueDetails
AHIS147
AGLU180
AHIS197
AHIS201
AHIS207
BHIS147
BASP149
BASP154
BGLY155
BASN157
BILE159
AASP149
BHIS162
BHIS175
BASP177
BGLU180
BHIS197
BHIS201
BHIS207
AASP154
AGLY155
AASN157
AILE159
AHIS162
AHIS175
AASP177

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN92
BASN92

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN184
AASN226
BASN184
BASN226

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

223532

PDB entries from 2024-08-07

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