Structure of PDB 5v7g Chain B Binding Site BS01
Receptor Information
>5v7g Chain B (length=317) Species:
266834
(Sinorhizobium meliloti 1021) [
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RPRILVPGKINPRVLERLPEMFETVRIERADAALVTADMRDVSGIAVSGK
LPVPLMDAFPSLEIVANFGVGYDGVDVSRAAARGIVVTNTPDVLTEEVAD
TAIGLLLNTLRLLPQAEQWLRQGRWVREGAFPLSPLSLRGRTVGLFGLGR
IGLAIARRLEAFGVSIAYHTRTPREGLGFTYHPTLVGMAEAVDTLIVIVP
GTASTLKAVNADVLSALGPKGVLINVGRGSTVDEAALVTALQNGTIAGAG
LDVFENEPNVPEALLSFPNVSLLPHVASASVVTRNAMSDLVVDNLKAWFS
TGEALTPVAETPFRRRA
Ligand information
Ligand ID
OXL
InChI
InChI=1S/C2H2O4/c3-1(4)2(5)6/h(H,3,4)(H,5,6)/p-2
InChIKey
MUBZPKHOEPUJKR-UHFFFAOYSA-L
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
[O-]C(=O)C([O-])=O
OpenEye OEToolkits 1.5.0
C(=O)(C(=O)[O-])[O-]
Formula
C2 O4
Name
OXALATE ION
ChEMBL
DrugBank
ZINC
PDB chain
5v7g Chain B Residue 401 [
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Receptor-Ligand Complex Structure
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PDB
5v7g
Structural, Biochemical, and Evolutionary Characterizations of Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two Distinct Subfamilies.
Resolution
1.75 Å
Binding residue
(original residue number in PDB)
G71 V72 G73 R230 H277
Binding residue
(residue number reindexed from 1)
G69 V70 G71 R228 H275
Annotation score
2
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.
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
View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB
RCSB:5v7g
,
PDBe:5v7g
,
PDBj:5v7g
PDBsum
5v7g
PubMed
29309127
UniProt
Q92LZ4
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