› 1clh

Solution NMR

THREE-DIMENSIONAL SOLUTION STRUCTURE OF ESCHERICHIA COLI PERIPLASMIC CYCLOPHILIN

Released:
DOI: 10.2210/pdb1clh/pdb
PDB entry 1clh coloured by chain, ensemble of 12 models, front view.
PDB entry 1clh coloured by chain, ensemble of 12 models, side view.
PDB entry 1clh coloured by chain, ensemble of 12 models, top view.
Source organism: Escherichia coli
Primary publication:
Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin.
Clubb RT, Ferguson SB, Walsh CT, Wagner G
Biochemistry 33 2761-72 (1994)
PMID: 8130188

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142738 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase A Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.1 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0AFL3 (Residues: 25-190; Coverage: 100%)
Gene names: JW3326, b3363, ppiA, rot, rotA
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

8 review citations

Peptidylproline cis/trans isomerases.
Galat et al. (1995)
7 more

6 mentions without citation

Application of sparse NMR restraints to large-scale protein structure prediction.
Li et al. (2004)
5 more