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1GXW

the 2.2 A resolution structure of thermolysin crystallized in presence of potassium thiocyanate

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 1317
ChainResidue
AASP138
AGLU177
AASP185
AGLU187
AGLU190
AHOH2100

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1318
ChainResidue
AGLU190
AHOH2108
AHOH2109
AGLU177
AASN183
AASP185

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1319
ChainResidue
AASP57
AASP59
AGLN61
AHOH2014
AHOH2041
AHOH2052

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1320
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH2107
AHOH2112

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1321
ChainResidue
AHIS142
AHIS146
AGLU166
ASCN1322

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN A 1322
ChainResidue
ATYR157
AGLU166
AHIS231
AZN1321
AHOH2169

site_idAC7
Number of Residues10
DetailsBinding site for Di-peptide VAL A 322 and LYS A 323
ChainResidue
AASN111
AASN112
AALA113
APHE130
AGLU143
ALEU202
AARG203
AHIS231
AHOH2169
AHOH2170

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

226707

PDB entries from 2024-10-30

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