› 1lep

X-ray diffraction
3.5Å resolution

THREE-DIMENSIONAL STRUCTURE OF THE IMMUNODOMINANT HEAT-SHOCK PROTEIN CHAPERONIN-10 OF MYCOBACTERIUM LEPRAE

Released:
DOI: 10.2210/pdb1lep/pdb
PDB entry 1lep coloured by chain, front view.
PDB entry 1lep coloured by chain, side view.
PDB entry 1lep coloured by chain, top view.
Source organism: Mycobacterium leprae
Primary publication:
Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae.
Mande SC, Mehra V, Bloom BR, Hol WG
Science 271 203-7 (1996)
PMID: 8539620

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-150205 (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 leprae
UniProt:
  • Canonical: P24301 (Residues: 2-100; Coverage: 99%)
Gene names: B1620_C3_227, B229_C3_247, ML0380, chpA, groES, groS, mopB
Sequence domains: Chaperonin 10 Kd subunit

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 112.9Å b: 129Å c: 109.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.23 0.38

Quick links

Citations

27 review citations

Molecular chaperones in cellular protein folding.
Hartl FU. (1996)
26 more

3 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
2 more