› 4h51

X-ray diffraction
1.85Å resolution

Crystal structure of a putative Aspartate Aminotransferase from Leishmania major Friedlin

Released:
DOI: 10.2210/pdb4h51/pdb
PDB entry 4h51 coloured by chain, front view.
PDB entry 4h51 coloured by chain, side view.
PDB entry 4h51 coloured by chain, top view.
Source organism: Leishmania major strain Friedlin
Primary publication:
Structures of aspartate aminotransferases from Trypanosoma brucei, Leishmania major and Giardia lamblia.
Abendroth J, Choi R, Wall A, Clifton MC, Lukacs CM, Staker BL, Van Voorhis W, Myler P, Lorimer DD, Edwards TE
Acta Crystallogr F Struct Biol Commun 71 566-71 (2015)
PMID: 25945710

Function and Biology Details

Reaction catalysed: 
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175522 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminotransferase class I/classII domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 420 amino acids
Theoretical weight: 47.3 KDa
Source organism: Leishmania major strain Friedlin
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q4FX34 (Residues: 1-412; Coverage: 100%)
Gene names: LMJF_35_0820, asat
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand EDO 2 x EDO
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P21
Unit cell:
a: 61.41Å b: 93.67Å c: 74.59Å
α: 90° β: 106.57° γ: 90°
R-values:
R R work R free
0.17 0.168 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

The Uptake and Metabolism of Amino Acids, and Their Unique Role in the Biology of Pathogenic Trypanosomatids.
Marchese et al. (2018)
1 more

3 mentions without citation

Mitochondrial selfish elements and the evolution of biological novelties.
Milani et al. (2016)
2 more