MolNFT v1 · #74362 · protein
PHD2-R127 with JNJ41536014
3OUH · Egl nine homolog 1: “PHD2-R127 with JNJ41536014”. X-ray diffraction, 3 ligands (014, FE2, SO4), 1 pocket (best druggability 0.62). MolNFT v1 #74362 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3OUH
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Egl nine homolog 1
- EC
- 1.14.11.-
- UniProt
- Q9GZT9
- Ligands
- 014, FE2, SO4
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Egl nine homolog 1 (EC 1.14.11.-) | protein | 212 | 28% helix, 31% strand | Q9GZT9 |
Ligands and binding sites
- 014 · 1-(5-chloro-6-fluoro-1H-benzimidazol-2-yl)-1H-pyrazole-4-carboxylic acid · ligand · chains A
- FE2 · Fe (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 117 | 0.62 | 0.86 | 25 | FE2, 014 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q9GZT9
- Elsewhere: RCSB PDB 3OUH · PDBe 3OUH · UniProt Q9GZT9
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