Research workbench
Structure of nitrite bound to reduced alcaligenes faecalis nitrite reductase at cryo temperature
Analyse Structure of nitrite bound to reduced alcaligenes faecalis nitrite reductase at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AS8
- Type
- protein
- Length
- 1,008 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitrite reductase
- EC
- 1.7.99.3
- UniProt
- P38501
- Ligands
- CU, NO2
- Pockets
- 12 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Nitrite reductase (EC 1.7.99.3) | protein | 336 | 11% helix, 43% strand | P38501 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 6 copies · chains A, B, C
- NO2 · Nitrite ion · ion · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 285 | 0.84 | 0.95 | 29 | empty |
| 2 | 521 | 0.80 | 0.87 | 57 | empty |
| 3 | 66 | 0.73 | 0.98 | 17 | empty |
| 4 | 65 | 0.72 | 0.97 | 18 | empty |
| 5 | 53 | 0.70 | 0.98 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2118 Ų buried · 33 hydrogen bonds · protein-protein
- B–C · 2105 Ų buried · 35 hydrogen bonds · protein-protein
- A–C · 2099 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 1AS8 · Structure of nitrite bound to reduced alcaligenes faecalis nitrite reductase at cryo… · the same entry in another collection · chain A against A, TM-score 1.00
- P38501 · AlphaFold monomer V2.0 prediction for copper-containing nitrite reductase (P38501) · a predicted model of the same protein · 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 P38501
- Elsewhere: RCSB PDB 1AS8 · PDBe 1AS8 · UniProt P38501
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.