Structure of PDB 1dpg Chain A

Receptor sequence
>1dpgA (length=485) Species: 1245 (Leuconostoc mesenteroides) [Search protein sequence]
VSEIKTLVTFFGGTGDLAKRKLYPSVFNLYKKGYLQKHFAIVGTARQALN
DDEFKQLVRDCIKDFTDDQAQAEAFIEHFSYRAHDVTDAASYAVLKEAIE
EAADKFDIDGNRIFYMSVAPRFFGTIAKYLKSEGLLADTGYNRLMIEKPF
GTSYDTAAELQNDLENAFDDNQLFRIDHYLGKEMVQNIAALRFGNPIFDA
AWNKDYIKNVQVTLSEVLGVEERAGYYDTAGALLDMIQNHTMQIVGWLAM
EKPESFTDKDIRAAKNAAFNALKIYDEAEVNKYFVRAQYGAGDSADFKPY
LEELDVPADSKNNTFIAGELQFDLPRWEGVPFYVRSGKRLAAKQTRVDIV
FKAGTFNFGSEQEAQEAVLSIIIDPKGAIELKLNAKSVEDAFNTRTIDLG
WTVSDEDKKNTPEPYERMIHDTMNGDGSNFADWNGVSIAWKFVDAISAVY
TADKAPLETYKSGSMGPEASDKLLAANGDAWVFKG
3D structure
PDB1dpg The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0 A resolution.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D177 H178 H240
Catalytic site (residue number reindexed from 1) D177 H178 H240
Enzyme Commision number 1.1.1.363: glucose-6-phosphate dehydrogenase [NAD(P)(+)].
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 PO4 A E147 K148 D177 H178 E147 K148 D177 H178
BS02 PO4 A H178 Y179 K182 H178 Y179 K182
Gene Ontology
Molecular Function
GO:0004345 glucose-6-phosphate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
GO:0050661 NADP binding
Biological Process
GO:0006006 glucose metabolic process
GO:0006098 pentose-phosphate shunt
GO:0009051 pentose-phosphate shunt, oxidative branch
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1dpg, PDBe:1dpg, PDBj:1dpg
PDBsum1dpg
PubMed7881907
UniProtP11411|G6PD_LEUME Glucose-6-phosphate 1-dehydrogenase (Gene Name=zwf)

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