Research workbench
Crystal structure of a high affinity heterodimer of HIF2 alpha and arnt C-terminal pas domains
Analyse Crystal structure of a high affinity heterodimer of HIF2 alpha and arnt… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F1P
- Type
- protein
- Length
- 225 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endothelial pas domain-containing protein 1; Aryl hydrocarbon receptor nuclear…
- UniProt
- Q99814, P27540
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endothelial pas domain-containing protein 1 | protein | 114 | 30% helix, 39% strand | Q99814 |
| B | Aryl hydrocarbon receptor nuclear translocator | protein | 111 | 21% helix, 36% strand | P27540 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.73 | 0.98 | 24 | empty |
| 2 | 67 | 0.40 | 0.80 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1006 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3F1P · Crystal structure of a high affinity heterodimer of HIF2 alpha and ARNT C-terminal PAS… · the same entry in another collection · chain A against A, TM-score 1.00
- P27540 · AlphaFold monomer V2.0 prediction for aryl hydrocarbon receptor nuclear translocator… · a predicted model of the same protein · chain B against A, TM-score 0.95
- Q99814 · AlphaFold monomer V2.0 prediction for endothelial pas domain- containing protein 1… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q99814
- Every structure of UniProt P27540
- Elsewhere: RCSB PDB 3F1P · PDBe 3F1P · UniProt Q99814 · UniProt P27540
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