› 2rqs

Solution NMR

3D structure of Pin from the psychrophilic archeon Cenarcheaum symbiosum (CsPin)

Released:
DOI: 10.2210/pdb2rqs/pdb
PDB entry 2rqs coloured by chain, ensemble of 20 models, front view.
PDB entry 2rqs coloured by chain, ensemble of 20 models, side view.
PDB entry 2rqs coloured by chain, ensemble of 20 models, top view.
Source organism: Cenarchaeum symbiosum
Primary publication:
Structure and dynamics of the first archaeal parvulin reveal a new functionally important loop in parvulin-type prolyl isomerases.
Jaremko Ł, Jaremko M, Elfaki I, Mueller JW, Ejchart A, Bayer P, Zhukov I
J Biol Chem 286 6554-65 (2011)
PMID: 21138844

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130769 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
peptidylprolyl isomerase Chain: A
Molecule details ›
Chain: A
Length: 97 amino acids
Theoretical weight: 10.52 KDa
Source organism: Cenarchaeum symbiosum
Expression system: Escherichia coli
UniProt:
  • Canonical: O74049 (Residues: 1-92; Coverage: 100%)
Gene names: CENSYa_1183, pinA
Sequence domains: PPIC-type PPIASE domain
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.
Hanes SD. (2014)
1 more

7 mentions without citation

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)
6 more