Structure of PDB 2dbq Chain A

Receptor sequence

>2dbqA (length=333) Species: 53953 (Pyrococcus horikoshii)

MKPKVFITREIPEVGIKMLEDEFEVEVWGDEKEIPREILLKKVKEVDALV
TMLSERIDKEVFENAPKLRIVANYAVGYDNIDIEEATKRGIYVTNTPDVL
TDATADLAFALLLATARHVVKGDRFVRSGEWKKRGVAWHPKWFLGYDVYG
KTIGIIGLGRIGQAIAKRAKGFNMRILYYSRTRKEEVERELNAEFKPLED
LLRESDFVVLAVPLTRETYHLINEERLKLMKKTAILINIARGKVVDTNAL
VKALKEGWIAGAGLDVFEEEPYYNEELFKLDNVVLTPHIGSASFGAREGM
AELVAKNLIAFKRGEIPPTLVNREVIKIRKPGF

3D structure

• PDB: 2dbq Structure of archaeal glyoxylate reductase from Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphate.
• Chain: A
• Resolution: 1.7 Å

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

External links

• PDB: RCSB:2dbq, PDBe:2dbq, PDBj:2dbq
• PDBsum: 2dbq
• PubMed: 17327673
• UniProt: O58320|GYAR_PYRHO Glyoxylate reductase (Gene Name=gyaR)