› 3pr9

X-ray diffraction
1.95Å resolution

Structural analysis of protein folding by the Methanococcus jannaschii chaperone FKBP26

Released:
DOI: 10.2210/pdb3pr9/pdb
PDB entry 3pr9 coloured by chain, front view.
PDB entry 3pr9 coloured by chain, side view.
PDB entry 3pr9 coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii
Primary publication:
Structural analysis of protein folding by the long-chain archaeal chaperone FKBP26.
Martinez-Hackert E, Hendrickson WA
J Mol Biol 407 450-64 (2011)
PMID: 21262232

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176587 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Long-type peptidyl-prolyl cis-trans isomerase Chain: A
Molecule details ›
Chain: A
Length: 157 amino acids
Theoretical weight: 17.51 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q58235 (Residues: 1-150; Coverage: 65%)
Gene name: MJ0825
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P3121
Unit cell:
a: 41.394Å b: 41.394Å c: 178.422Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.209 0.269
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Solution NMR studies on Helicobacter pylori proteins for antibiotic target discovery.
Lee et al. (2016)
3 other articles

2 mentions without citation

Structural analysis of protein folding by the long-chain archaeal chaperone FKBP26.
Martinez-Hackert et al. (2011)
1 more