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2JSD

Solution structure of MMP20 complexed with NNGH

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 273
ChainResidue
AASP183
AGLY184
AARG186
ATHR188
AASP206
AGLU209

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 274
ChainResidue
AGLU197
AGLY198
AGLY200
AASP202
AGLU164
AALA165
AASP166

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 275
ChainResidue
AHIS176
AASP178
AHIS191
AHIS204

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 276
ChainResidue
AHIS226
AHIS230
AHIS236
ANGH277

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NGH A 277
ChainResidue
AGLY187
ATHR188
ALEU189
AALA190
ATHR222
AHIS226
AGLU227
AHIS230
AHIS236
ATYR245
APRO246
ATHR247
ATYR248
ALYS249
AZN276

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHAL
ChainResidueDetails
AVAL223-LEU232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095
ChainResidueDetails
AGLU227

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING:
ChainResidueDetails
AGLU164
AHIS191
AGLU197
AGLY198
AGLY200
AASP202
AHIS204
AASP206
AGLU209
AHIS226
AHIS230
AALA165
AHIS236
AASP166
AHIS176
AASP178
AASP183
AGLY184
AARG186
ATHR188

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU227
AMET244

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1hfs
ChainResidueDetails
AGLU227

224004

PDB entries from 2024-08-21

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