MolNFT v1 · #179938 · protein
Crystal structure of S. cerevisiae ESS1
7KKF · Peptidyl-prolyl cis-trans isomerase ESS1: “Crystal structure of S. cerevisiae ESS1”. X-ray diffraction, 1 pocket (best druggability 0.35). MolNFT v1 #179938 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7KKF
- Type
- protein
- Length
- 293 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase ESS1
- EC
- 5.2.1.8
- UniProt
- A0A6L0ZJ56
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase ESS1 (EC 5.2.1.8) | protein | 162 | 25% helix, 22% strand | A0A6L0ZJ56 |
| B | Peptidyl-prolyl cis-trans isomerase ESS1 (EC 5.2.1.8) | protein | 131 | 31% helix, 18% strand | A0A6L0ZJ56 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.35 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 238 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 7KKF · Crystal Structure of S. cerevisiae Ess1 · 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 A0A6L0ZJ56
- Elsewhere: RCSB PDB 7KKF · PDBe 7KKF · UniProt A0A6L0ZJ56
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