Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P11411","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues26
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P11413","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon