Research workbench
Crystal structure of selective IRE1a inhibitor 29 at the enzyme active site
Analyse Crystal structure of selective IRE1a inhibitor 29 at the enzyme active site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8UVL
- Type
- protein
- Length
- 403 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.43
- Source
- Homo sapiens
- Molecule
- Serine/threonine-protein kinase/endoribonuclease IRE1
- EC
- 2.7.11.1, 3.1.26.-
- UniProt
- O75460
- Ligands
- XOE
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · resolution 2.43 · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine/threonine-protein kinase/endoribonuclease IRE1 (EC 2.7.11.1, 3.1.26.-) | protein | 403 | 46% helix, 14% strand | O75460 |
Ligands and binding sites
- XOE · 1-phenyl-N-(2,3,6-trifluoro-4-{[(3M)-3-(2-{[(3R,5R)-5-fluoropiperidin-3-yl]amino}pyrimidin-4-yl)pyridin-2-yl]oxy}phenyl)methanesulfonamide · ligand · chains A
- EDO · 1,2-ethanediol · additive · 8 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 438 | 0.73 | 0.83 | 42 | XOE |
| 2 | 108 | 0.51 | 0.82 | 20 | empty |
| 3 | 192 | 0.50 | 0.76 | 27 | EDO |
| 4 | 51 | 0.27 | 0.74 | 12 | EDO |
Compared structures
- O75460 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein KINASE/ENDORIBONUCLEASE… · 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 O75460
- Elsewhere: RCSB PDB 8UVL · PDBe 8UVL · UniProt O75460
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