› 1rmh

X-ray diffraction
2.4Å resolution

RECOMBINANT CYCLOPHILIN A FROM HUMAN T CELL

Released:
DOI: 10.2210/pdb1rmh/pdb
PDB entry 1rmh coloured by chain, front view.
PDB entry 1rmh coloured by chain, side view.
PDB entry 1rmh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization.
Zhao Y, Ke H
Biochemistry 35 7356-61 (1996)
PMID: 8652511

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:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158806 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 164 amino acids
Theoretical weight: 17.91 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P62937 (Residues: 2-165; Coverage: 99%)
Gene names: CYPA, PPIA
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like
AAPF PEPTIDE SUBSTRATE Chains: C, D
Molecule details ›
Chains: C, D
Length: 6 amino acids
Theoretical weight: 625 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 37.8Å b: 109.2Å c: 118.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Not provided

Quick links

Citations

5 review citations

Coupled motions in enzyme catalysis.
Nashine et al. (2010)
4 more

11 mentions without citation

New targets for HIV drug discovery.
Puhl et al. (2019)
10 more