Structure of PDB 1jdj Chain A

Receptor sequence
>1jdjA (length=346) Species: 5665 (Leishmania mexicana) [Search protein sequence]
KDELLYLNKAVVFGSGAFGTALAMVLSKKCREVCVWHMNEEEVRLVNEKR
ENVLFLKGVQLASNITFTSDVEKAYNGAEIILFVIPTQFLRGFFEKSGGN
LIAYAKEKQVPVLVCTKGIERSTLKFPAEIIGEFLPSPLLSVLAGPSFAI
EVATGVFTCVSIASADINVARRLQRIMSTGDRSFVCWATTDTVGCEVASA
VKNVLAIGSGVANGLGMGLNARAALIMRGLLEIRDLTAALGGDGSAVFGL
AGLGDLQLTCSSELSRNFTVGKKLGKGLPIEEIQRAVAEGVATADPLMRL
AKQLKVKMPLCHQIYEIVYKKKNPRDALADLLSCGLQDEGLPPLFK
3D structure
PDB1jdj Anomalous differences of light elements in determining precise binding modes of ligands to glycerol-3-phosphate dehydrogenase.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K210 T267
Catalytic site (residue number reindexed from 1) K202 T259
Enzyme Commision number 1.1.1.8: glycerol-3-phosphate dehydrogenase (NAD(+)).
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 CFP A W44 M46 F97 W36 M38 F89 PDBbind-CN: -logKd/Ki=2.30,IC50=5mM
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0051287 NAD binding
GO:0141152 glycerol-3-phosphate dehydrogenase (NAD+) activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006072 glycerol-3-phosphate metabolic process
GO:0006116 NADH oxidation
GO:0046168 glycerol-3-phosphate catabolic process
Cellular Component
GO:0005829 cytosol
GO:0020015 glycosome

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1jdj, PDBe:1jdj, PDBj:1jdj
PDBsum1jdj
PubMed12445769
UniProtP90551|GPDA_LEIME Glycerol-3-phosphate dehydrogenase [NAD(+)], glycosomal (Gene Name=GPD)

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