Research workbench
Factor inhibiting hif-1 alpha in complex with hif-1 alpha fragment peptide
Analyse Factor inhibiting hif-1 alpha in complex with hif-1 alpha fragment peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H2L
- Type
- protein
- Length
- 354 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Factor inhibiting HIF1; Hypoxia-inducible factor 1 alpha
- UniProt
- Q969Q7, Q16665
- Ligands
- AKG, FE2, SO4
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Factor inhibiting HIF1 | protein | 332 | 31% helix, 25% strand | Q969Q7 |
| S | Hypoxia-inducible factor 1 alpha | protein | 22 | 32% helix, 0% strand | Q16665 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · chains A
- FE2 · Fe (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 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 | 76 | 0.73 | 0.97 | 22 | FE2, AKG |
| 2 | 152 | 0.47 | 0.77 | 32 | empty |
| 3 | 92 | 0.46 | 0.80 | 28 | empty |
| 4 | 135 | 0.43 | 0.75 | 26 | empty |
| 5 | 93 | 0.41 | 0.78 | 20 | empty |
Interfaces
1 interface between chains.
- A–S · 1368 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 1H2L · Factor Inhibiting HIF-1 alpha in complex with HIF-1 alpha fragment peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q16665 · AlphaFold monomer V2.0 prediction for hypoxia-inducible factor 1-alpha (Q16665) · a predicted model of the same protein · chain S against A, TM-score 0.32
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 Q969Q7
- Every structure of UniProt Q16665
- Elsewhere: RCSB PDB 1H2L · PDBe 1H2L · UniProt Q969Q7 · UniProt Q16665
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