Research workbench
Human cyclophilin a complexed with THR2, LEU5, D-HIV8, LEU10 cyclosporin
Analyse Human cyclophilin a complexed with THR2, LEU5, D-HIV8, LEU10 cyclosporin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CWO
- Type
- protein
- Length
- 175 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase a; Cyclosporin C
- EC
- 5.2.1.8
- UniProt
- P62937
- Ligands
- VAD
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8) | protein | 165 | 14% helix, 33% strand | P62937 |
| C | Cyclosporin C | protein | 10 | 0% helix, 10% strand | — |
Ligands and binding sites
- VAD · Deaminohydroxyvaline · ligand · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–C · 508 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified, 2 covalent (nonstandard, covalent ligand, methylation).
Compared structures
- 1CWO · Human cyclophilin a complexed with THR2, LEU5, D-HIV8, LEU10 cyclosporin · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P62937
- Elsewhere: RCSB PDB 1CWO · PDBe 1CWO · UniProt P62937
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