Research workbench
Factor inhibiting hif-1 alpha
Analyse Factor inhibiting hif-1 alpha in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H2N
- Type
- protein
- Length
- 332 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
- AKG, FE2, SO4
- Pockets
- 5 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypoxia-inducible factor 1-alpha inhibitor (EC 1.14.11.16) | protein | 332 | 31% helix, 27% strand | Q9NWT6 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · chains A
- FE2 · Fe (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.66 | 0.84 | 28 | AKG |
| 2 | 96 | 0.45 | 0.79 | 23 | empty |
| 3 | 129 | 0.41 | 0.75 | 26 | empty |
| 4 | 85 | 0.32 | 0.73 | 19 | empty |
| 5 | 55 | 0.25 | 0.73 | 14 | empty |
Compared structures
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 1H2N · PDBe 1H2N · UniProt Q9NWT6
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