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2OY4

Uninhibited human MMP-8

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
F0004222molecular_functionmetalloendopeptidase activity
F0006508biological_processproteolysis
F0008237molecular_functionmetallopeptidase activity
F0008270molecular_functionzinc ion binding
F0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 996
ChainResidue
AASP137
AGLY169
AGLY171
AASP173
AHOH1018
AHOH1038

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

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

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 999
ChainResidue
AHIS197
AHIS201
AHIS207
AHOH1095
AHOH1140
AHOH1143

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA F 996
ChainResidue
FASP137
FGLY169
FGLY171
FASP173
FHOH1050
FHOH1064

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA F 997
ChainResidue
FASP154
FGLY155
FASN157
FILE159
FASP177
FGLU180

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 998
ChainResidue
FHIS147
FASP149
FHIS162
FHIS175

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 999
ChainResidue
FHIS197
FHIS201
FHIS207
FHOH1072

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
FGLU198

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AASP137
AGLY169
AGLY171
AASP173
FASP137
FGLY169
FGLY171
FASP173

site_idSWS_FT_FI3
Number of Residues26
DetailsBINDING: BINDING => ECO:0000269|PubMed:8137810
ChainResidueDetails
AHIS147
AGLU180
AHIS197
AHIS201
AHIS207
FHIS147
FASP149
FASP154
FGLY155
FASN157
FILE159
AASP149
FHIS162
FHIS175
FASP177
FGLU180
FHIS197
FHIS201
FHIS207
AASP154
AGLY155
AASN157
AILE159
AHIS162
AHIS175
AASP177

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN92
FASN92

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN184
AASN226
FASN184
FASN226

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
FMET215
FGLU198

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
FGLU198

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PDB entries from 2024-07-24

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