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Crystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin a
Analyse Crystal structure of murine cyclophilin C complexed with immunosuppressive drug… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RMC
- Type
- protein
- Length
- 772 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase C; Cyclosporin a
- EC
- 5.2.1.8
- UniProt
- P30412
- Pockets
- 9 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | Peptidyl-prolyl cis-trans isomerase C (EC 5.2.1.8) | protein | 182 | 13% helix, 38% strand | P30412 |
| B, D, F, H | Cyclosporin a | protein | 11 | 0% helix, 9% strand | — |
Pockets
9 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 405 | 0.65 | 0.79 | 60 | empty |
| 2 | 111 | 0.47 | 0.80 | 30 | empty |
| 3 | 165 | 0.43 | 0.74 | 22 | empty |
| 4 | 163 | 0.43 | 0.74 | 21 | empty |
| 5 | 105 | 0.42 | 0.77 | 25 | empty |
Interfaces
10 interfaces between chains.
- A–B · 497 Ų buried · 6 hydrogen bonds · protein-protein
- G–H · 495 Ų buried · 6 hydrogen bonds · protein-protein
- E–F · 494 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 491 Ų buried · 6 hydrogen bonds · protein-protein
- E–G · 444 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 modified, 4 d-amino (nonstandard, methylation, D-amino acid).
Compared structures
- 2RMC · Crystal structure of murine cyclophilin C complexed with immunosuppressive drug… · the same entry in another collection · chain H against H, TM-score 1.00
- P30412 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase C (P30412) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P30412
- Elsewhere: RCSB PDB 2RMC · PDBe 2RMC · UniProt P30412
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