› 5hxw

X-ray diffraction
2.63Å resolution

L-amino acid deaminase from Proteus vulgaris

Released:
DOI: 10.2210/pdb5hxw/pdb
PDB entry 5hxw coloured by chain, front view.
PDB entry 5hxw coloured by chain, side view.
PDB entry 5hxw coloured by chain, top view.
Source organism: Proteus vulgaris
Primary publication:
Crystal structure of a membrane-bound l-amino acid deaminase from Proteus vulgaris.
Ju Y, Tong S, Gao Y, Zhao W, Liu Q, Gu Q, Xu J, Niu L, Teng M, Zhou H
J Struct Biol 195 306-315 (2016)
PMID: 27422658

Function and Biology Details

Reaction catalysed: 
An L-amino acid + H(2)O + O(2) = a 2-oxo carboxylate + NH(3) + H(2)O(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192251 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD dependent oxidoreductase domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 454 amino acids
Theoretical weight: 50.08 KDa
Source organism: Proteus vulgaris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9LCB2 (Residues: 30-471; Coverage: 94%)
Gene name: LAD
Sequence domains: FAD dependent oxidoreductase

Ligands and Environments


Cofactor: Ligand FAD 6 x FAD
1 bound ligand:
Ligand 16A 15 x 16A
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 3W1A
Spacegroup: P1
Unit cell:
a: 100.314Å b: 104.575Å c: 105.419Å
α: 64.52° β: 73.06° γ: 61.17°
R-values:
R R work R free
0.223 0.221 0.252
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Breaking the mirror: l-Amino acid deaminase, a novel stereoselective biocatalyst.
Molla et al. (2017)
2 more

4 mentions without citation

Membrane binding of the insertion sequence of Proteus vulgaris L-amino acid deaminase stabilizes protein structure and increases catalytic activity.
Ju et al. (2017)
3 more