› 4cbr

X-ray diffraction
2.3Å resolution

X-ray structure of the more stable human AGXT triple mutant (AGXT_HEM)

Released:
DOI: 10.2210/pdb4cbr/pdb
PDB entry 4cbr coloured by chain, front view.
PDB entry 4cbr coloured by chain, side view.
PDB entry 4cbr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The consensus-based approach for gene/enzyme replacement therapies and crystallization strategies: the case of human alanine-glyoxylate aminotransferase.
Mesa-Torres N, Yunta C, Fabelo-Rosa I, Gonzalez-Rubio JM, Sánchez-Ruiz JM, Salido E, Albert A, Pey AL
Biochem J 462 453-63 (2014)
PMID: 24957194

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 Chain: A
Molecule details ›
Chain: A
Length: 392 amino acids
Theoretical weight: 43.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P21549 (Residues: 1-392; Coverage: 100%)
Gene names: AGT1, AGXT, SPAT
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P41212
Unit cell:
a: 90.2Å b: 90.2Å c: 140.99Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.22 0.268
Expression system: Escherichia coli BL21

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Citations

5 review citations

Molecular basis of primary hyperoxaluria: clues to innovative treatments.
Dindo et al. (2019)
4 more