› 1i1k

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE.

Released:
DOI: 10.2210/pdb1i1k/pdb
PDB entry 1i1k coloured by chain, front view.
PDB entry 1i1k coloured by chain, side view.
PDB entry 1i1k coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structures of Escherichia coli branched-chain amino acid aminotransferase and its complexes with 4-methylvalerate and 2-methylleucine: induced fit and substrate recognition of the enzyme.
Okada K, Hirotsu K, Hayashi H, Kagamiyama H
Biochemistry 40 7453-63 (2001)
PMID: 11412098

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 hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142021 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Branched-chain-amino-acid aminotransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 309 amino acids
Theoretical weight: 34.13 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AB80 (Residues: 1-309; Coverage: 100%)
Gene names: JW5606, b3770, ilvE
Sequence domains: Amino-transferase class IV
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 3 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200H
Spacegroup: C2221
Unit cell:
a: 100.93Å b: 156.06Å c: 141.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.231
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Dual substrate recognition of aminotransferases.
Hirotsu et al. (2005)
4 more

1 mention without citation

Structural Consideration of the Working Mechanism of Fold Type I Transaminases From Eubacteria: Overt and Covert Movement.
Kwon et al. (2019)