› 1hx5

X-ray diffraction
3.5Å resolution

Crystal structure of M. tuberculosis chaperonin-10

Released:
DOI: 10.2210/pdb1hx5/pdb
PDB entry 1hx5 coloured by chain, front view.
PDB entry 1hx5 coloured by chain, side view.
PDB entry 1hx5 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Three-dimensional Structure of Mycobacterium tuberculosis Chaperonin-10 Reveals a Partially Stable Conformation for its Mobile Loop
Taneja B, Mande SC
Curr. Sci. 81 87-91 (2001)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161972 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Co-chaperonin GroES Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 99 amino acids
Theoretical weight: 10.68 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPE5 (Residues: 2-100; Coverage: 99%)
Gene names: MTCY78.11, Rv3418c, cpn10, groES, groS, mopB
Sequence domains: Chaperonin 10 Kd subunit
Structure domains: GroES chaperonin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2221
Unit cell:
a: 77.5Å b: 162.5Å c: 125.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.265
Expression system: Escherichia coli

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Citations

2 mentions without citation

A histidine-rich and cysteine-rich metal-binding domain at the C terminus of heat shock protein A from Helicobacter pylori: implication for nickel homeostasis and bismuth susceptibility.
Cun et al. (2008)
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