Research workbench
Cryptosporidium parvum cyclophilin type peptidyl-prolyl cis-trans isomerase CGD2_4120 in complex with cyclosporin a
Analyse Cryptosporidium parvum cyclophilin type peptidyl-prolyl cis-trans isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2POY
- Type
- protein
- Length
- 541 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase; Cyclosporin a
- UniProt
- A3FQA7
- Pockets
- 4 · best druggability 0.49
Structure
x-ray diffraction · 3 distinct chains · 13% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Peptidyl-prolyl cis-trans isomerase | protein | 168 | 14% helix, 32% strand | A3FQA7 |
| B | Peptidyl-prolyl cis-trans isomerase | protein | 172 | 13% helix, 33% strand | A3FQA7 |
| T, U, V | Cyclosporin a | protein | 11 | 0% helix, 9% strand | — |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.49 | 0.80 | 20 | empty |
| 2 | 96 | 0.38 | 0.75 | 22 | empty |
| 3 | 79 | 0.35 | 0.76 | 17 | empty |
| 4 | 52 | 0.23 | 0.71 | 17 | empty |
Interfaces
8 interfaces between chains.
- A–T · 518 Ų buried · 8 hydrogen bonds · protein-protein
- B–U · 510 Ų buried · 7 hydrogen bonds · protein-protein
- C–V · 506 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 378 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 256 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified, 3 d-amino (nonstandard, methylation, D-amino acid).
Compared structures
- 2POY · Cryptosporidium parvum cyclophilin type peptidyl-prolyl cis-trans isomerase cgd2_4120 in… · 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 A3FQA7
- Elsewhere: RCSB PDB 2POY · PDBe 2POY · UniProt A3FQA7
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