PDBe 1ekf

X-ray diffraction
1.95Å resolution

CRYSTALLOGRAPHIC STRUCTURE OF HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL) COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE AT 1.95 ANGSTROMS (ORTHORHOMBIC FORM)

Released:
Source organism: Homo sapiens
Primary publication:
The structure of human mitochondrial branched-chain aminotransferase.
Acta Crystallogr. D Biol. Crystallogr. 57 506-15 (2001)
PMID: 11264579

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Branched-chain-amino-acid aminotransferase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 365 amino acids
Theoretical weight: 41.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15382 (Residues: 28-392; Coverage: 93%)
Gene names: BCAT2, BCATM, BCT2, ECA40
Sequence domains: Amino-transferase class IV
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: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 69.385Å b: 105.032Å c: 107.016Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.222 0.26
Expression system: Escherichia coli BL21(DE3)