Research workbench
The X-ray structure of (MEBM2T)1-cyclosporin complexed with cyclophilin a provides an explanation for its anomalously high immunosuppressive activity
Analyse The X-ray structure of (MEBM2T)1-cyclosporin complexed with cyclophilin a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CWB
- Type
- protein
- Length
- 176 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase a; Cyclosporin a
- EC
- 5.2.1.8
- UniProt
- P05092
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 32% 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, 34% strand | P05092 |
| C | Cyclosporin a | protein | 11 | 0% helix, 9% strand | — |
Interfaces
1 interface between chains.
- A–C · 510 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified, 1 d-amino (nonstandard, methylation, D-amino acid).
Compared structures
- 1CWB · The X-ray structure of (MEBM2T)1-cyclosporin complexed with cyclophilin a provides an… · 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 P05092
- Elsewhere: RCSB PDB 1CWB · PDBe 1CWB · UniProt P05092
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