› 2vhz

X-ray diffraction
2.04Å resolution

Crystal structure of holo L-alanine dehydrogenase from Mycobacterium tuberculosis in the closed conformation

Released:
DOI: 10.2210/pdb2vhz/pdb
PDB entry 2vhz coloured by chain, front view.
PDB entry 2vhz coloured by chain, side view.
PDB entry 2vhz coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Three-dimensional structures of apo- and holo-L-alanine dehydrogenase from Mycobacterium tuberculosis reveal conformational changes upon coenzyme binding.
Agren D, Stehr M, Berthold CL, Kapoor S, Oehlmann W, Singh M, Schneider G
J Mol Biol 377 1161-73 (2008)
PMID: 18304579

Function and Biology Details

Reaction catalysed: 
L-alanine + H(2)O + NAD(+) = pyruvate + NH(3) + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162061 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alanine dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 377 amino acids
Theoretical weight: 39.58 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WQB1 (Residues: 1-371; Coverage: 100%)
Gene names: MTV002.45, Rv2780, ald
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAI 2 x NAI
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P213
Unit cell:
a: 140.991Å b: 140.991Å c: 140.991Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Enzymatic asymmetric synthesis of chiral amino acids.
Xue et al. (2018)
2 more

1 mention without citation

Domain Motions and Functionally-Key Residues of L-Alanine Dehydrogenase Revealed by an Elastic Network Model.
Li et al. (2015)