› 4i8a

X-ray diffraction
2.9Å resolution

Function and Biology Details

Reactions catalysed: 
L-alanine + glyoxylate = pyruvate + glycine
L-serine + pyruvate = 3-hydroxypyruvate + L-alanine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149289 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alanine--glyoxylate aminotransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 394 amino acids
Theoretical weight: 43.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P21549 (Residues: 1-392; Coverage: 100%)
Gene names: AGT1, AGXT, SPAT
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 13 x GOL
1 modified residue:
Ligand LLP 4 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P21
Unit cell:
a: 78.892Å b: 101.564Å c: 116.749Å
α: 90° β: 90.64° γ: 90°
R-values:
R R work R free
0.253 0.251 0.278
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

The chaperone role of the pyridoxal 5'-phosphate and its implications for rare diseases involving B6-dependent enzymes.
Cellini et al. (2014)
1 more

2 mentions without citation

Crystal structure of the S187F variant of human liver alanine: glyoxylate [corrected] aminotransferase associated with primary hyperoxaluria type I and its functional implications.
Oppici et al. (2013)
1 more