› 2zp7

X-ray diffraction
2.26Å resolution

Crystal structure of LysN, alpha-aminoadipate aminotransferase (Leucine complex), from Thermus thermophilus HB27

Released:
DOI: 10.2210/pdb2zp7/pdb
PDB entry 2zp7 coloured by chain, front view.
PDB entry 2zp7 coloured by chain, side view.
PDB entry 2zp7 coloured by chain, top view.
Source organism: Thermus thermophilus HB27
Primary publication:
Mechanism for multiple-substrates recognition of alpha-aminoadipate aminotransferase from Thermus thermophilus.
Tomita T, Miyagawa T, Miyazaki T, Fushinobu S, Kuzuyama T, Nishiyama M
Proteins 75 348-59 (2009)
PMID: 18831049

Function and Biology Details

Reaction catalysed: 
L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180893 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-aminoadipate transaminase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 397 amino acids
Theoretical weight: 43.9 KDa
Source organism: Thermus thermophilus HB27
Expression system: Escherichia coli
UniProt:
  • Canonical: Q72LL6 (Residues: 1-397; Coverage: 100%)
Gene names: TT_C0043, lysN
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 6 x PLP
1 bound ligand:
Ligand LEU 3 x LEU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 55.948Å b: 167.639Å c: 119.358Å
α: 90° β: 97.87° γ: 90°
R-values:
R R work R free
0.208 0.205 0.263
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structure, expression, and function of kynurenine aminotransferases in human and rodent brains.
Han et al. (2010)
1 more

1 mention without citation

Crystal structure of L-aspartate aminotransferase from Schizosaccharomyces pombe.
Jeong et al. (2019)