Function and Biology Details
Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158799 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase A
Molecule details ›
Chains: A, B
Length: 165 amino acids
Theoretical weight: 18.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like
Length: 165 amino acids
Theoretical weight: 18.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P62937 (Residues: 1-165; Coverage: 100%)
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like
HIV-1 Capsid
Molecule details ›
Chains: C, D
Length: 146 amino acids
Theoretical weight: 16.2 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: gag protein p24 N-terminal domain
Structure domains: Human Immunodeficiency Virus Type 1 Capsid Protein
Length: 146 amino acids
Theoretical weight: 16.2 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q72497 (Residues: 133-278; Coverage: 29%)
Sequence domains: gag protein p24 N-terminal domain
Structure domains: Human Immunodeficiency Virus Type 1 Capsid Protein
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ALS BEAMLINE 5.0.2
Spacegroup:
P21
Expression system: Escherichia coli BL21(DE3)
