› 4uoc

X-ray diffraction
2.46Å resolution

Competence or damage-inducible protein CinA from Thermus thermophilus

Released:
DOI: 10.2210/pdb4uoc/pdb
PDB 4uoc coloured by chain and viewed from the front.
PDB 4uoc coloured by chain and viewed from the side.
PDB 4uoc coloured by chain and viewed from the top.
Source organism: Thermus thermophilus HB8
Primary publication:
Structure and Mechanism of the Bifunctional CinA Enzyme from Thermus thermophilus.
Karuppiah V, Thistlethwaite A, Dajani R, Warwicker J, Derrick JP
J. Biol. Chem. (2014)
PMID: 25313401

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CinA-like protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 394 amino acids
Theoretical weight: 43.04 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q5SHB0 (Residues: 1-394; Coverage: 100%)
Gene name: TTHA1820
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NCN 2 x NCN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 72.47Å b: 93.3Å c: 133.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.25
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Protocol for Computational Enzymatic Reactivity Based on Geometry Optimisation.
Cerqueira et al. (2018)
1 more

2 mentions without citation

Structure and mechanism of the bifunctional CinA enzyme from Thermus thermophilus.
Karuppiah et al. (2014)
1 more