Research workbench
Factor inhibiting hif-1 alpha in complex with R-2-hydroxyglutarate
Analyse Factor inhibiting hif-1 alpha in complex with R-2-hydroxyglutarate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YC0
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypoxia-inducible factor 1-alpha inhibitor
- EC
- 1.14.11.16
- UniProt
- Q9NWT6
- Ligands
- 2HG, FE2, SO4
- Pockets
- 4 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypoxia-inducible factor 1-alpha inhibitor (EC 1.14.11.16) | protein | 349 | 31% helix, 25% strand | Q9NWT6 |
Ligands and binding sites
- 2HG · (2R)-2-hydroxypentanedioic acid · ligand · chains A
- FE2 · Fe (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
- GOL · Glycerol · additive · 3 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 247 | 0.66 | 0.83 | 32 | FE2, 2HG, GOL |
| 2 | 91 | 0.47 | 0.81 | 25 | GOL |
| 3 | 90 | 0.38 | 0.76 | 22 | empty |
| 4 | 86 | 0.33 | 0.74 | 21 | empty |
Compared structures
- 2YC0 · Factor inhibiting hif-1 alpha in complex with R-2-hydroxyglutarate · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NWT6 · AlphaFold monomer V2.0 prediction for hypoxia-inducible factor 1-alpha inhibitor (Q9NWT6) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q9NWT6
- Elsewhere: RCSB PDB 2YC0 · PDBe 2YC0 · UniProt Q9NWT6
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