Research workbench
Factor inhibiting hif (fih) in complex with zinc and vadadustat
Analyse Factor inhibiting hif (fih) in complex with zinc and vadadustat in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OPC
- Type
- protein
- Length
- 339 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypoxia-inducible factor 1-alpha inhibitor
- EC
- 1.14.11.30, 1.14.11.-
- UniProt
- Q9NWT6
- Ligands
- A1Z, ZN, SO4
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypoxia-inducible factor 1-alpha inhibitor (EC 1.14.11.30, 1.14.11.-) | protein | 339 | 30% helix, 25% strand | Q9NWT6 |
Ligands and binding sites
- A1Z · Vadadustat · ligand · chains A
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · 5 copies · chains A
- GOL · Glycerol · additive · 5 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 | 329 | 0.68 | 0.82 | 40 | ZN, GOL, A1Z |
| 2 | 78 | 0.44 | 0.81 | 19 | GOL |
| 3 | 128 | 0.42 | 0.75 | 23 | empty |
| 4 | 67 | 0.28 | 0.73 | 16 | empty |
Compared structures
- 5OPC · Factor Inhibiting HIF (FIH) in complex with zinc and Vadadustat · 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 0.95
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 5OPC · PDBe 5OPC · UniProt Q9NWT6
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