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8EM2

Cryo-EM structure of the human GDH/6PGL endoplasmic bifunctional protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0004345molecular_functionglucose-6-phosphate dehydrogenase activity
A0005975biological_processcarbohydrate metabolic process
A0006006biological_processglucose metabolic process
A0006098biological_processpentose-phosphate shunt
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0017057molecular_function6-phosphogluconolactonase activity
A0050661molecular_functionNADP binding
B0004345molecular_functionglucose-6-phosphate dehydrogenase activity
B0005975biological_processcarbohydrate metabolic process
B0006006biological_processglucose metabolic process
B0006098biological_processpentose-phosphate shunt
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0017057molecular_function6-phosphogluconolactonase activity
B0050661molecular_functionNADP binding
Functional Information from PROSITE/UniProt
site_idPS00069
Number of Residues7
DetailsG6P_DEHYDROGENASE Glucose-6-phosphate dehydrogenase active site. DHYLGKQ
ChainResidueDetails
AASP203-GLN209

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P11411","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P11413","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8CFX1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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