› 1vjo

X-ray diffraction
1.7Å resolution

Function and Biology Details

Reaction catalysed: 
L-alanine + glyoxylate = pyruvate + glycine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187142 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminotransferase class V domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 393 amino acids
Theoretical weight: 43.75 KDa
Source organism: Nostoc sp. PCC 7120 = FACHB-418
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8YY48 (Residues: 1-381; Coverage: 100%)
Gene name: alr1004
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
No bound ligands
1 modified residue:
Ligand MSE 8 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2221
Unit cell:
a: 79.258Å b: 101.057Å c: 97.252Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.151 0.202
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Human wild-type alanine:glyoxylate aminotransferase and its naturally occurring G82E variant: functional properties and physiological implications.
Cellini et al. (2007)
5 more

4 mentions without citation

On the combination of molecular replacement and single-wavelength anomalous diffraction phasing for automated structure determination.
Panjikar et al. (2009)
3 more