› 1iyd

X-ray diffraction
2.15Å resolution

CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE

Released:
DOI: 10.2210/pdb1iyd/pdb
PDB entry 1iyd coloured by chain, front view.
PDB entry 1iyd coloured by chain, side view.
PDB entry 1iyd coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of branched-chain amino acid aminotransferase complexed with glutamate and glutarate: true reaction intermediate and double substrate recognition of the enzyme.
Goto M, Miyahara I, Hayashi H, Kagamiyama H, Hirotsu K
Biochemistry 42 3725-33 (2003)
PMID: 12667063

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
1 bound ligand:
Ligand GUA 3 x GUA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2221
Unit cell:
a: 154.27Å b: 99.02Å c: 138.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.242
Expression system: Escherichia coli

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Citations

7 review citations

Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
Eliot et al. (2004)
6 more