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7E6I

Glucose-6-phosphate dehydrogenase in complex with its substrate glucose-6-phosphate

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 PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue BG6 A 501
ChainResidue
ALYS153
AHOH700
AHIS183
ATYR184
ALYS187
AGLU221
AASP240
AHIS245
ALYS339
AGLN373

site_idAC2
Number of Residues3
Detailsbinding site for residue TRS A 502
ChainResidue
AGLU397
AHOH608
AHOH614

site_idAC3
Number of Residues7
Detailsbinding site for residue 7PE A 503
ChainResidue
ATHR395
AGLU397
AASP399
AHOH611
AHOH633
AHOH634
AHOH634

Functional Information from PROSITE/UniProt
site_idPS00069
Number of Residues7
DetailsG6P_DEHYDROGENASE Glucose-6-phosphate dehydrogenase active site. DHYLGKE
ChainResidueDetails
AASP182-GLU188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P11411
ChainResidueDetails
AHIS245

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P11413
ChainResidueDetails
AGLY15
AARG49
ALYS153
AHIS183
AGLU221
AASP240
ALYS339
AGLN373

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PDB entries from 2024-06-26

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