1ekv

X-ray diffraction
2.25Å resolution

HUMAN BRANCHED CHAIN AMINO ACID AMINOTRANSFERASE (MITOCHONDRIAL): THREE DIMENSIONAL STRUCTURE OF ENZYME INACTIVATED BY TRIS BOUND TO THE PYRIDOXAL-5'-PHOSPHATE ON ONE END AND ACTIVE SITE LYS202 NZ ON THE OTHER.

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)
PDBe Complex ID:
PDB-CPX-127454 (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
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P32
Unit cell:
a: 83.74Å b: 83.74Å c: 104.81Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.231 0.189 0.25
Expression system: Escherichia coli BL21(DE3)