› 1aws

X-ray diffraction
2.55Å resolution

SECYPA COMPLEXED WITH HAGPIA (PSEUDO-SYMMETRIC MONOMER)

Released:
DOI: 10.2210/pdb1aws/pdb
PDB entry 1aws coloured by chain, front view.
PDB entry 1aws coloured by chain, side view.
PDB entry 1aws coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.
Vajdos FF, Yoo S, Houseweart M, Sundquist WI, Hill CP
Protein Sci 6 2297-307 (1997)
PMID: 9385632

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158770 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase A Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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
PEPTIDE FROM THE HIV-1 CAPSID PROTEIN Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 566 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P43
Unit cell:
a: 51.9Å b: 51.9Å c: 63.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.262 0.262 0.337
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

10 review citations

Retrovirus restriction factors.
Goff SP. (2004)
9 more

1 mention without citation

A statistical mechanical method to optimize energy functions for protein folding.
Bastolla et al. (2000)