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1PE5

Thermolysin with tricyclic inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 317
ChainResidue
AHIS142
AHIS146
AGLU166
ABR3322

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 318
ChainResidue
AHOH346
AASP138
AGLU177
AASP185
AGLU187
AGLU190

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 319
ChainResidue
AGLU177
AASN183
AASP185
AGLU190
AHOH353
AHOH475

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 320
ChainResidue
AASP57
AASP59
AGLN61
AHOH419
AHOH482
AHOH503

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 321
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH354
AHOH480

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BR3 A 322
ChainResidue
AASN112
AALA113
AHIS142
AGLU143
AHIS146
ATYR157
AGLU166
AASP226
AHIS231
AZN317
ALEU323
ALEN324
AHOH549

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE LEU A 323
ChainResidue
AASN112
AALA113
AGLU143
ALEU202
AARG203
AHIS231
ABR3322
ALEN324

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LEN A 324
ChainResidue
AASN112
ALEU202
ABR3322
ALEU323

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_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1tlp
ChainResidueDetails
AHIS231
AGLU143

site_idMCSA1
Number of Residues
DetailsM-CSA 176
ChainResidueDetails

224931

PDB entries from 2024-09-11

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