Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3DPE

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 996
ChainResidue
AASP137
AGLY169
AGLY171
AASP173
AHOH1158

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

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 Residues26
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
AHOH1030
AHOH1040
AHOH1052
AHOH1065
AHOH1138
AHOH1179
AHOH1194

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AMET215
AGLU198

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU198

221716

PDB entries from 2024-06-26

PDB statisticsPDBj update infoContact PDBjnumon