MolNFT v1 · #19545 · protein
Plasmodium falciparum cyclophilin (double mutant) complexed with cyclosporin a
1QNH · Peptidyl-prolyl cis-trans isomerase: “Plasmodium falciparum cyclophilin (double mutant) complexed with cyclosporin a”. X-ray diffraction, 2 pockets (best druggability 0.50). MolNFT v1 #19545 on GenesisL1: 3D structure, binding sites…
- PDB
- 1QNH
- Type
- protein
- Length
- 361 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase; Cyclosporin a
- EC
- 5.2.1.8
- UniProt
- Q25756
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 3 distinct chains · 13% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 169 | 14% helix, 34% strand | Q25756 |
| B | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 170 | 14% helix, 34% strand | Q25756 |
| C, D | Cyclosporin a | protein | 11 | 0% helix, 9% strand | — |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 199 | 0.50 | 0.76 | 27 | empty |
| 2 | 110 | 0.43 | 0.78 | 19 | empty |
Interfaces
3 interfaces between chains.
- B–D · 496 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 493 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 474 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified, 2 d-amino (nonstandard, methylation, D-amino acid).
Compared structures
- 1QNH · Plasmodium falciparum Cyclophilin (double mutant) complexed with Cyclosporin A · 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 Q25756
- Elsewhere: RCSB PDB 1QNH · PDBe 1QNH · UniProt Q25756
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