› 5f9s

X-ray diffraction
1.7Å resolution

Crystal structure of human Alanine:Glyoxylate Aminotransferase major allele (AGT-Ma) at 1.7 Angstrom; internal aldimine with PLP in the active site

Released:
DOI: 10.2210/pdb5f9s/pdb
PDB entry 5f9s coloured by chain, front view.
PDB entry 5f9s coloured by chain, side view.
PDB entry 5f9s coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Radiation damage at the active site of human alanine:glyoxylate aminotransferase reveals that the cofactor position is finely tuned during catalysis.
Giardina G, Paiardini A, Montioli R, Cellini B, Voltattorni CB, Cutruzzolà F
Sci Rep 7 11704 (2017)
PMID: 28916765

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: 386 amino acids
Theoretical weight: 42.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21549 (Residues: 6-391; Coverage: 99%)
Gene names: AGT1, AGXT, SPAT
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P212121
Unit cell:
a: 54.479Å b: 101.88Å c: 131.338Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.205
Expression system: Escherichia coli

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Citations

7 citation in other articles

The catalytic activity of serine hydroxymethyltransferase is essential for de novo nuclear dTMP synthesis in lung cancer cells.
Giardina et al. (2018)
6 more

4 mentions without citation

Radiation damage at the active site of human alanine:glyoxylate aminotransferase reveals that the cofactor position is finely tuned during catalysis.
Giardina et al. (2017)
3 more