› 2a6p

X-ray diffraction
2.2Å resolution

Structure Solution to 2.2 Angstrom and Functional Characterisation of the Open Reading Frame Rv3214 from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb2a6p/pdb
PDB entry 2a6p coloured by chain, front view.
PDB entry 2a6p coloured by chain, side view.
PDB entry 2a6p coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase.
Watkins HA, Baker EN
J Bacteriol 188 3589-99 (2006)
PMID: 16672613

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181470 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglycerate mutase family protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 22.43 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7D5X2 (Residues: 26-228; Coverage: 89%)
Gene name: MT3310
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 44.343Å b: 79.844Å c: 52.839Å
α: 90° β: 109.11° γ: 90°
R-values:
R R work R free
0.209 0.209 0.226
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Structural genomics as an approach towards understanding the biology of tuberculosis.
Baker EN. (2007)
1 more

3 mentions without citation

Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase.
Watkins et al. (2006)
2 more