3k5p

X-ray diffraction
2.15Å resolution

Crystal structure of amino acid-binding ACT: D-isomer specific 2-hydroxyacid dehydrogenase catalytic domain from Brucella melitensis

Released:
Source organism: Brucella abortus 2308
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reactions catalysed:
(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH
3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-174155 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-3-phosphoglycerate dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 416 amino acids
Theoretical weight: 45.03 KDa
Source organism: Brucella abortus 2308
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2YK82 (Residues: 1-412; Coverage: 100%)
Gene names: BAB2_0783, serA-2
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P6222
Unit cell:
a: 97.891Å b: 97.891Å c: 189.215Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.182 0.216
Expression system: Escherichia coli