PDBe 5bwr

X-ray diffraction
2.2Å resolution

X-RAY CRYSTAL STRUCTURE AT 2.20A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A PYRAZOLOPYRIMIDINONE FRAGMENT AND AN INTERNAL ALDIMINE LINKED PLP.

Released:

Function and Biology Details

Reaction catalysed:
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
Biochemical function:
Biological process:
Cellular component:

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: 369 amino acids
Theoretical weight: 41.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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
3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 69.165Å b: 106.214Å c: 107.454Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.173 0.234
Expression system: Escherichia coli