Research workbench
The crystal structure of the saccharomyces cerevisiae co-chaperone CPR7
Analyse The crystal structure of the saccharomyces cerevisiae co-chaperone CPR7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JHE
- Type
- protein
- Length
- 388 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase CYP7
- EC
- 5.2.1.8
- UniProt
- P47103
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase CYP7 (EC 5.2.1.8) | protein | 388 | 42% helix, 16% strand | P47103 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.51 | 0.80 | 26 | empty |
| 2 | 54 | 0.30 | 0.76 | 18 | empty |
| 3 | 55 | 0.28 | 0.74 | 13 | empty |
Compared structures
- 5JHE · The Crystal Structure of the Saccharomyces cerevisiae Co-Chaperone Cpr7 · the same entry in another collection · chain A against A, TM-score 1.00
- P47103 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase CYP7 (P47103) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P47103
- Elsewhere: RCSB PDB 5JHE · PDBe 5JHE · UniProt P47103
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