› 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:
DOI: 10.2210/pdb1ekf/pdb
PDB entry 1ekf coloured by chain, front view.
PDB entry 1ekf coloured by chain, side view.
PDB entry 1ekf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of human mitochondrial branched-chain aminotransferase.
Yennawar N, Dunbar J, Conway M, Hutson S, Farber G
Acta Crystallogr D Biol Crystallogr 57 506-15 (2001)
PMID: 11264579

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
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
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)

Quick links

Citations

1 review citation

Genome-scale metabolic models as platforms for identification of novel genes as antimicrobial drug targets.
Mienda et al. (2018)
21 other articles

1 mention without citation

Structural Basis for Allostery in PLP-dependent Enzymes.
Tran et al. (2022)