› 2h5x

X-ray diffraction
2.7Å resolution

RuvA from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb2h5x/pdb
PDB entry 2h5x coloured by chain, front view.
PDB entry 2h5x coloured by chain, side view.
PDB entry 2h5x coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.
Prabu JR, Thamotharan S, Khanduja JS, Alipio EZ, Kim CY, Waldo GS, Terwilliger TC, Segelke B, Lekin T, Toppani D, Hung LW, Yu M, Bursey E, Muniyappa K, Chandra NR, Vijayan M
Acta Crystallogr Sect F Struct Biol Cryst Commun 62 731-4 (2006)
PMID: 16880543

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161524 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Holliday junction branch migration complex subunit RuvA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 196 amino acids
Theoretical weight: 20.21 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P9WGW3 (Residues: 1-196; Coverage: 100%)
Gene names: MTCY227.08, Rv2593c, ruvA
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P42212
Unit cell:
a: 137.642Å b: 137.642Å c: 88.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.233 0.272
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

The eradication of leprosy: molecular modeling techniques for novel drug discovery.
Anusuya et al. (2013)
1 other article

3 mentions without citation

Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases.
Husain et al. (2010)
2 more