› 1o6y

X-ray diffraction
2.2Å resolution

Catalytic domain of PknB kinase from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb1o6y/pdb
PDB entry 1o6y coloured by chain, front view.
PDB entry 1o6y coloured by chain, side view.
PDB entry 1o6y coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis.
Ortiz-Lombardía M, Pompeo F, Boitel B, Alzari PM
J Biol Chem 278 13094-100 (2003)
PMID: 12551895

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161604 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase PknB Chain: A
Molecule details ›
Chain: A
Length: 299 amino acids
Theoretical weight: 32.46 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WI81 (Residues: 1-279; Coverage: 45%)
Gene names: MTCY10H4.14c, Rv0014c, pknB
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ACP 1 x ACP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2221
Unit cell:
a: 114.607Å b: 122.088Å c: 46.975Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.23
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

19 review citations

Eukaryote-like serine/threonine kinases and phosphatases in bacteria.
Pereira et al. (2011)
18 more

19 mentions without citation

Substrate and docking interactions in serine/threonine protein kinases.
Goldsmith et al. (2007)
18 more