Research workbench
Prolyl hydroxylase in complex with hypoxia inducible factor oxygen degradation domain peptide fragment from trichoplax adhaerens
Analyse Prolyl hydroxylase in complex with hypoxia inducible factor oxygen degradation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F0W
- Type
- protein
- Length
- 238 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hif prolyl hydroxylase; Hypoxia inducible factor, alpha subunit
- UniProt
- I6QVT6, I6QP75
- Ligands
- OGA, MN
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hif prolyl hydroxylase | protein | 220 | 30% helix, 32% strand | I6QVT6 |
| S | Hypoxia inducible factor, alpha subunit | protein | 18 | 39% helix, 17% strand | I6QP75 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.76 | 0.99 | 22 | OGA, MN |
| 2 | 89 | 0.39 | 0.77 | 16 | empty |
| 3 | 61 | 0.27 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–S · 1062 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, oxidation).
Compared structures
- 6F0W · prolyl hydroxylase in complex with hypoxia inducible factor oxygen degradation domain… · the same entry in another collection · chain A against A, TM-score 1.00
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 I6QVT6
- Every structure of UniProt I6QP75
- Elsewhere: RCSB PDB 6F0W · PDBe 6F0W · UniProt I6QVT6 · UniProt I6QP75
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