› 2jek

X-ray diffraction
1.38Å resolution

Crystal structure of the conserved hypothetical protein Rv1873 from Mycobacterium tuberculosis at 1.38 A

Released:
DOI: 10.2210/pdb2jek/pdb
PDB entry 2jek coloured by chain, front view.
PDB entry 2jek coloured by chain, side view.
PDB entry 2jek coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
The molecular structure of Rv1873, a conserved hypothetical protein from Mycobacterium tuberculosis, at 1.38 A resolution.
Garen CR, Cherney MM, Bergmann EM, James MN
Acta Crystallogr Sect F Struct Biol Cryst Commun 62 1201-5 (2006)
PMID: 17142896

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126607 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Calpastatin Chain: A
Molecule details ›
Chain: A
Length: 145 amino acids
Theoretical weight: 16.23 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: O07756 (Residues: 1-145; Coverage: 100%)
Gene name: Rv1873
Sequence domains: Protein of unknown function (DUF1810)
Structure domains: Protein of unknown function DUF1810

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 33.44Å b: 31.627Å c: 53.187Å
α: 90° β: 90.8° γ: 90°
R-values:
R R work R free
0.169 0.167 0.2
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Genomic characteristics of Mycobacterium tuberculosis isolates of cutaneous tuberculosis.
Mei et al. (2023)

1 mention without citation

Statistical dictionaries for hypothetical in silico model of the early-stage intermediate in protein folding.
Kalinowska et al. (2015)