› 2yob

X-ray diffraction
1.9Å 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
Molecule details ›
Chains: A, B
Length: 388 amino acids
Theoretical weight: 42.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P21549 (Residues: 1-388; Coverage: 99%)
Gene names: AGT1, AGXT, SPAT
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
3 bound ligands:
Ligand BTB 2 x BTB
Ligand SO4 2 x SO4
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 54.495Å b: 103.525Å c: 153.832Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.17 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Innovative strategies to treat protein misfolding in inborn errors of metabolism: pharmacological chaperones and proteostasis regulators.
Muntau et al. (2014)
7 more

2 mentions without citation

The role of protein denaturation energetics and molecular chaperones in the aggregation and mistargeting of mutants causing primary hyperoxaluria type I.
Mesa-Torres et al. (2013)
1 more