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1E77

COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004345molecular_functionglucose-6-phosphate dehydrogenase activity
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006098biological_processpentose-phosphate shunt
A0009051biological_processpentose-phosphate shunt, oxidative branch
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0050661molecular_functionNADP binding
Functional Information from PROSITE/UniProt
site_idPS00069
Number of Residues7
DetailsG6P_DEHYDROGENASE Glucose-6-phosphate dehydrogenase active site. DHYLGKE
ChainResidueDetails
AASP177-GLU183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:9485426
ChainResidueDetails
ATHR241

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11320304, ECO:0000269|PubMed:9485426
ChainResidueDetails
AGLY13
AGLN47
AVAL86

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11320304
ChainResidueDetails
APRO149

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000305|PubMed:11106478
ChainResidueDetails
ATYR179
AGLU183
AVAL217
AMET236
AARG339
AGLN344

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dpg
ChainResidueDetails
AASP177
AHIS240

site_idMCSA1
Number of Residues3
DetailsM-CSA 843
ChainResidueDetails
AHIS178modifies pKa
ATYR179transition state stabiliser
ATHR241proton acceptor, proton donor

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PDB entries from 2024-10-30

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