MolNFT v1 · #148239 · protein
Prolyl hydroxylase in complex with hypoxia inducible factor oxygen degradation domain peptide fragment from trichoplax adhaerens
6F0W · Hif prolyl hydroxylase: “Prolyl hydroxylase in complex with hypoxia inducible factor oxygen degradation domain peptide fragment from…”. X-ray diffraction, 2 ligands (OGA, MN), 3 pockets (best druggability 0.76). MolNFT v1 #148239 on…
- 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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