PDBe 1j49

X-ray diffraction
2.2Å resolution

INSIGHTS INTO DOMAIN CLOSURE, SUBSTRATE SPECIFICITY AND CATALYSIS OF D-LACTATE DEHYDROGENASE FROM LACTOBACILLUS BULGARICUS

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-lactate dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 333 amino acids
Theoretical weight: 37.12 KDa
Source organism: Lactobacillus delbrueckii subsp. bulgaricus
Expression system: Escherichia coli
UniProt:
  • Canonical: P26297 (Residues: 1-333; Coverage: 100%)
Gene names: Ldb0101, ldhA
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P43212
Unit cell:
a: 79.4Å b: 79.4Å c: 228.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.271
Expression system: Escherichia coli