MolNFT v1 · #54888 · protein
S-nitrosylated PHD2 (no exposed) in complex with FE(II) and UN9
2Y34 · Egl nine homolog 1: “S-nitrosylated PHD2 (no exposed) in complex with FE(II) and UN9”. X-ray diffraction, 2 ligands (UN9, FE2), 1 pocket (best druggability 0.66). MolNFT v1 #54888 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2Y34
- Type
- protein
- Length
- 216 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
- UN9, FE2
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Egl nine homolog 1 (EC 1.14.11.-) | protein | 216 | 26% helix, 30% strand | Q9GZT9 |
Ligands and binding sites
- UN9 · N-[(1-chloro-4-hydroxyisoquinolin-3-yl)carbonyl]glycine · ligand · 2 copies · chains A
- FE2 · Fe (II) ion · metal · 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 | 121 | 0.66 | 0.88 | 21 | FE2, UN9 |
Modifications
Observed in the structure: 1 modified (nonstandard).
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 2Y34 · PDBe 2Y34 · UniProt Q9GZT9
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