MolNFT v1 · #100674 · protein
Nitrosomonas europea hao soaked in NH2OH
4N4O · Hydroxylamine oxidoreductase: “Nitrosomonas europea hao soaked in NH2OH”. X-ray diffraction, 4 ligands (HEC, HOA, K), 18 pockets (best druggability 0.91). MolNFT v1 #100674 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4N4O
- Type
- protein
- Length
- 1,674 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydroxylamine oxidoreductase
- EC
- 1.7.2.6
- UniProt
- Q50925, Q82V11
- Ligands
- HEC, HOA, K, PO4
- Pockets
- 18 · best druggability 0.91
Structure
x-ray diffraction · 6 distinct chains · 51% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydroxylamine oxidoreductase (EC 1.7.2.6) | protein | 504 | 51% helix, 2% strand | Q50925 |
| B | Hydroxylamine oxidoreductase (EC 1.7.2.6) | protein | 53 | 40% helix, 28% strand | Q82V11 |
| C | Hydroxylamine oxidoreductase (EC 1.7.2.6) | protein | 502 | 53% helix, 2% strand | Q50925 |
| D | Hydroxylamine oxidoreductase (EC 1.7.2.6) | protein | 57 | 35% helix, 26% strand | Q82V11 |
| E | Hydroxylamine oxidoreductase (EC 1.7.2.6) | protein | 503 | 52% helix, 2% strand | Q50925 |
| F | Hydroxylamine oxidoreductase (EC 1.7.2.6) | protein | 55 | 40% helix, 27% strand | Q82V11 |
Ligands and binding sites
- HEC · Heme C · ligand · 24 copies · chains A, C, E
- HOA · Hydroxyamine · ligand · 3 copies · chains A, C, E
- K · Potassium ion · metal · chains A, C, E
- PO4 · Phosphate ion · ion · chains E
- 12P · Dodecaethylene glycol · additive · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 821 | 0.91 | 0.95 | 147 | HEC, HOA |
| 2 | 621 | 0.90 | 0.95 | 105 | HEC |
| 3 | 338 | 0.86 | 0.95 | 58 | HEC |
| 4 | 564 | 0.84 | 0.90 | 53 | empty |
| 5 | 220 | 0.82 | 0.95 | 43 | HEC |
Interfaces
9 interfaces between chains.
- A–E · 2869 Ų buried · 33 hydrogen bonds · protein-protein
- C–E · 2855 Ų buried · 38 hydrogen bonds · protein-protein
- A–C · 2850 Ų buried · 41 hydrogen bonds · protein-protein
- C–D · 647 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 619 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 47 cofactor, 3 disulfide (heme c attachment, 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 Q50925
- Every structure of UniProt Q82V11
- Elsewhere: RCSB PDB 4N4O · PDBe 4N4O · UniProt Q50925 · UniProt Q82V11
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