Research workbench
Acetyl-CYPA:CYCLOSPORINE complex
Analyse Acetyl-CYPA:CYCLOSPORINE complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X2C
- Type
- protein
- Length
- 880 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclosporin a; Peptidyl-prolyl cis-trans isomerase a
- EC
- 5.2.1.8
- UniProt
- P62937
- Pockets
- 8 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, F, L, P, R | Cyclosporin a | protein | 11 | 0% helix, 0% strand | — |
| K, M, O, Q, S | Peptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8) | protein | 165 | 15% helix, 33% strand | P62937 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 316 | 0.56 | 0.75 | 37 | empty |
| 2 | 280 | 0.51 | 0.74 | 32 | empty |
| 3 | 192 | 0.50 | 0.77 | 28 | empty |
| 4 | 147 | 0.47 | 0.77 | 25 | empty |
| 5 | 106 | 0.47 | 0.80 | 19 | empty |
Interfaces
15 interfaces between chains.
- K–L · 511 Ų buried · 7 hydrogen bonds · protein-protein
- Q–R · 504 Ų buried · 6 hydrogen bonds · protein-protein
- O–P · 490 Ų buried · 6 hydrogen bonds · protein-protein
- O–Q · 375 Ų buried · 5 hydrogen bonds · protein-protein
- M–O · 342 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 45 modified, 5 d-amino (nonstandard, methylation, D-amino acid, acetylation).
Compared structures
- 2X2C · acetyl-CypA:cyclosporine complex · the same entry in another collection · chain B against B, 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 2X2C · PDBe 2X2C · UniProt P62937
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