Structure of PDB 5v7g Chain B

Receptor sequence
>5v7gB (length=317) Species: 266834 (Sinorhizobium meliloti 1021) [Search protein sequence]
RPRILVPGKINPRVLERLPEMFETVRIERADAALVTADMRDVSGIAVSGK
LPVPLMDAFPSLEIVANFGVGYDGVDVSRAAARGIVVTNTPDVLTEEVAD
TAIGLLLNTLRLLPQAEQWLRQGRWVREGAFPLSPLSLRGRTVGLFGLGR
IGLAIARRLEAFGVSIAYHTRTPREGLGFTYHPTLVGMAEAVDTLIVIVP
GTASTLKAVNADVLSALGPKGVLINVGRGSTVDEAALVTALQNGTIAGAG
LDVFENEPNVPEALLSFPNVSLLPHVASASVVTRNAMSDLVVDNLKAWFS
TGEALTPVAETPFRRRA
3D structure
PDB5v7g Structural, Biochemical, and Evolutionary Characterizations of Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two Distinct Subfamilies.
ChainB
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L96 R230 D254 E259 H277
Catalytic site (residue number reindexed from 1) L94 R228 D252 E257 H275
Enzyme Commision number 1.1.1.81: hydroxypyruvate 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 OXL B G71 V72 G73 R230 H277 G69 V70 G71 R228 H275
BS02 NDP B V72 G73 V100 L150 G151 R152 I153 T172 R173 V201 P202 S206 T207 V228 G229 R230 H277 A279 V70 G71 V98 L148 G149 R150 I151 T170 R171 V199 P200 S204 T205 V226 G227 R228 H275 A277
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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:0046872 metal ion binding
GO:0051287 NAD binding
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:5v7g, PDBe:5v7g, PDBj:5v7g
PDBsum5v7g
PubMed29309127
UniProtQ92LZ4

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