Function and Biology Details
Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain
- Retrovirus capsid, N-terminal
- Cyclophilin-like domain superfamily
- Retroviral nucleocapsid Gag protein p24, C-terminal domain
- Retrovirus capsid, C-terminal
- Retroviral nucleocapsid Gag protein p24, N-terminal
- Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site
- Cyclophilin-type peptidyl-prolyl cis-trans isomerase
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138042 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Capsid protein p24
Molecule details ›
Chains: A, B
Length: 218 amino acids
Theoretical weight: 24.35 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 218 amino acids
Theoretical weight: 24.35 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
- Canonical:
P04591 (Residues: 133-350; Coverage: 44%)
Sequence domains:
Peptidyl-prolyl cis-trans isomerase A
Molecule details ›
Chain: C
Length: 164 amino acids
Theoretical weight: 17.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Length: 164 amino acids
Theoretical weight: 17.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P62937 (Residues: 2-165; Coverage: 99%)
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
