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1KJP

Thermolysin complexed with Z-L-Glutamic acid (benzyloxycarbonyl-L-Glutamic acid)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP138
AGLU177
AASP185
AGLU187
AGLU190
AHOH1320

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AGLU190
AHOH1334
AHOH1345
AGLU177
AASN183
AASP185

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP57
AASP59
AGLN61
AHOH1329
AHOH1331
AHOH1336

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH1324
AHOH1366

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 405
ChainResidue
AHIS142
AHIS146
AGLU166
AGLU1317

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PHQ A 317
ChainResidue
AASN112
AALA113
AVAL139
AHIS142
AGLU143
AILE188
ALEU202
AGLU1317
AHOH1429

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GLU A 1317
ChainResidue
AASN112
AALA113
AHIS142
AGLU143
AHIS146
ATYR157
AGLU166
AHIS231
APHQ317
AZN405
AHOH1428

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV
ChainResidueDetails
AVAL139-VAL148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AVAL289
ASER291
ATHR293

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 176
ChainResidueDetails

218853

PDB entries from 2024-04-24

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