› 5lha

X-ray diffraction
1.89Å resolution

Amine transaminase crystal structure from an uncultivated Pseudomonas species in the PMP-bound form

Released:
DOI: 10.2210/pdb5lha/pdb
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PDB entry 5lha coloured by chain, front view.
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PDB entry 5lha coloured by chain, top view.
Source organism: Pseudomonas sp.
Primary publication:
Explaining Operational Instability of Amine Transaminases: Substrate-Induced Inactivation Mechanism and Influence of Quaternary Structure on Enzyme-Cofactor Intermediate Stability.
Borner T, Ramisch S, Reddem E, Bartsch S, Vogel A, Thunnissen AMWH, Adlercreutz P, Grey C
ACS Catalysis 7 1259-1269 (2017)

Function and Biology Details

Reaction catalysed: 
L-alanine + 3-oxopropanoate = pyruvate + beta-alanine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-103829 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Omega transaminase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 458 amino acids
Theoretical weight: 49.57 KDa
Source organism: Pseudomonas sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A1W2VMW5 (Residues: 1-434; Coverage: 100%)
Sequence domains: Aminotransferase class-III
Structure domains: Type I PLP-dependent aspartate aminotransferase-like (Major domain)

Ligands and Environments


Cofactor: Ligand PMP 4 x PMP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 96.79Å b: 97.069Å c: 153.389Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.172 0.225
Expression system: Escherichia coli

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