Research workbench
Nitrosomonas europea hao
Analyse Nitrosomonas europea hao in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4N4N
- Type
- protein
- Length
- 1,678 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, K, PO4
- Pockets
- 20 · best druggability 0.90
Structure
x-ray diffraction · 6 distinct chains · 50% 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 | 56 | 38% helix, 27% strand | Q82V11 |
| C | Hydroxylamine oxidoreductase (EC 1.7.2.6) | protein | 502 | 52% helix, 2% strand | Q50925 |
| D | Hydroxylamine oxidoreductase (EC 1.7.2.6) | protein | 57 | 40% 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 | 56 | 39% helix, 27% strand | Q82V11 |
Ligands and binding sites
- HEC · Heme C · ligand · 24 copies · chains A, C, E
- K · Potassium ion · metal · chains A, C, E
- PO4 · Phosphate ion · ion · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 651 | 0.90 | 0.95 | 115 | HEC |
| 2 | 347 | 0.86 | 0.95 | 57 | HEC |
| 3 | 783 | 0.85 | 0.88 | 64 | empty |
| 4 | 253 | 0.84 | 0.95 | 49 | HEC |
| 5 | 243 | 0.83 | 0.95 | 46 | HEC |
Interfaces
9 interfaces between chains.
- C–E · 2879 Ų buried · 34 hydrogen bonds · protein-protein
- A–E · 2860 Ų buried · 37 hydrogen bonds · protein-protein
- A–C · 2839 Ų buried · 38 hydrogen bonds · protein-protein
- E–F · 634 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 630 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 51 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 4N4N · PDBe 4N4N · UniProt Q50925 · UniProt Q82V11
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