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4QKZ

X-ray structure of the catalytic domain of MMP-8 with the inhibitor ML115

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 Residues6
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AASP137
AGLY169
AGLY171
AASP173
AHOH408
AHOH412

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 302
ChainResidue
AILE159
AASP177
AGLU180
AASP154
AGLY155
AASN157

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 303
ChainResidue
AHIS147
AASP149
AHIS162
AHIS175

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 304
ChainResidue
AHIS197
AHIS201
AHIS207
AQZK305

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE QZK A 305
ChainResidue
AILE159
ALEU160
AALA161
AHIS162
ALEU193
AHIS197
AGLU198
AHIS201
AHIS207
ALEU214
ATYR216
APRO217
AASN218
ATYR219
AZN304
AHOH415
AHOH424
AHOH450
AHOH451
AHOH464
AHOH504
AHOH506
AHOH507

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MES A 306
ChainResidue
AASP115
ASER186
APHE192
ATHR224
ASER225
ATYR227
AHOH428
AHOH478
AHOH533

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 Residues1
DetailsACT_SITE:
ChainResidueDetails
AGLU198

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AASP137
AGLY169
AGLY171
AASP173

site_idSWS_FT_FI3
Number of Residues13
DetailsBINDING: BINDING => ECO:0000269|PubMed:8137810
ChainResidueDetails
AHIS147
AGLU180
AHIS197
AHIS201
AHIS207
AASP149
AASP154
AGLY155
AASN157
AILE159
AHIS162
AHIS175
AASP177

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN92

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN184
AASN226

218853

PDB entries from 2024-04-24

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