› 2o0r

X-ray diffraction
2Å resolution

The three-dimensional structure of N-Succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb2o0r/pdb
PDB entry 2o0r coloured by chain, front view.
PDB entry 2o0r coloured by chain, side view.
PDB entry 2o0r coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
The three-dimensional structure of N-succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis.
Weyand S, Kefala G, Weiss MS
J Mol Biol 367 825-38 (2007)
PMID: 17292400

Function and Biology Details

Reaction catalysed: 
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-2-L-amino-6-oxoheptanedioate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162033 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable N-succinyldiaminopimelate aminotransferase DapC Chains: A, B
Molecule details ›
Chains: A, B
Length: 411 amino acids
Theoretical weight: 44.09 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPZ5 (Residues: 2-397; Coverage: 100%)
Gene names: Rv0858c, dapC
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CL 2 x CL
Ligand GOL 2 x GOL
Ligand NA 1 x NA
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P2221
Unit cell:
a: 54.34Å b: 56.13Å c: 247.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.164 0.213
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Inhibition of lysine biosynthesis: an evolving antibiotic strategy.
Hutton et al. (2007)
2 more

2 mentions without citation

L,L-diaminopimelate aminotransferase from Chlamydomonas reinhardtii: a target for algaecide development.
Dobson et al. (2011)
1 more