Research workbench
Peptidyl-prolyl isomerase ESS1 from candida albicans
Analyse Peptidyl-prolyl isomerase ESS1 from candida albicans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YW5
- Type
- protein
- Length
- 177 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl prolyl CIS/TRANS isomerase
- EC
- 5.2.1.8
- UniProt
- Q9C475
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl prolyl CIS/TRANS isomerase (EC 5.2.1.8) | protein | 177 | 29% helix, 21% strand | Q9C475 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.36 | 0.77 | 21 | empty |
| 2 | 68 | 0.33 | 0.75 | 13 | empty |
Compared structures
- 1YW5 · Peptidyl-prolyl isomerase ESS1 from Candida albicans · 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 Q9C475
- Elsewhere: RCSB PDB 1YW5 · PDBe 1YW5 · UniProt Q9C475
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