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BioLiP

Structure of PDB 2dbq Chain A

Receptor sequence
>2dbqA (length=333) Species: 53953 (Pyrococcus horikoshii) [Search protein sequence]
MKPKVFITREIPEVGIKMLEDEFEVEVWGDEKEIPREILLKKVKEVDALV
TMLSERIDKEVFENAPKLRIVANYAVGYDNIDIEEATKRGIYVTNTPDVL
TDATADLAFALLLATARHVVKGDRFVRSGEWKKRGVAWHPKWFLGYDVYG
KTIGIIGLGRIGQAIAKRAKGFNMRILYYSRTRKEEVERELNAEFKPLED
LLRESDFVVLAVPLTRETYHLINEERLKLMKKTAILINIARGKVVDTNAL
VKALKEGWIAGAGLDVFEEEPYYNEELFKLDNVVLTPHIGSASFGAREGM
AELVAKNLIAFKRGEIPPTLVNREVIKIRKPGF
3D structure
PDB2dbq Structure of archaeal glyoxylate reductase from Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphate.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L100 R241 D265 E270 H288
Catalytic site (residue number reindexed from 1) L100 R241 D265 E270 H288
Enzyme Commision number 1.1.1.26: glyoxylate reductase.
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 NAP A V76 T104 L158 G159 R160 I161 S180 R181 T182 A211 V212 P213 T218 I239 A240 R241 D265 H288 G290 V76 T104 L158 G159 R160 I161 S180 R181 T182 A211 V212 P213 T218 I239 A240 R241 D265 H288 G290
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:0016618 hydroxypyruvate reductase [NAD(P)H] activity
GO:0030267 glyoxylate reductase (NADPH) activity
GO:0047964 glyoxylate reductase (NADH) activity
GO:0051287 NAD binding
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:2dbq, PDBe:2dbq, PDBj:2dbq
PDBsum2dbq
PubMed17327673
UniProtO58320|GYAR_PYRHO Glyoxylate reductase (Gene Name=gyaR)

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