MolNFT v1 · #15888 · protein
The structure of cu-nitrite reductase from achromobacter cycloclastes at five pH values, with nitrite bound and with type II cu depleted
1NIF: “The structure of cu-nitrite reductase from achromobacter cycloclastes at five pH values, with nitrite bound…”. X-ray diffraction, 1 ligand (CU), 2 pockets (best druggability 0.77). MolNFT v1 #15888 on GenesisL1: 3D structure…
- PDB
- 1NIF
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitrite reductase
- EC
- 1.7.99.3
- UniProt
- P25006
- Ligands
- CU
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitrite reductase (EC 1.7.99.3) | protein | 333 | 11% helix, 41% strand | P25006 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 101 | 0.77 | 0.97 | 21 | empty |
| 2 | 52 | 0.36 | 0.79 | 17 | empty |
Compared structures
- 1NIF · The structure of cu-nitrite reductase from achromobacter cycloclastes at five pH values… · the same entry in another collection · chain A against A, TM-score 1.00
- P25006 · AlphaFold monomer V2.0 prediction for copper-containing nitrite reductase (P25006) · 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 P25006
- Elsewhere: RCSB PDB 1NIF · PDBe 1NIF · UniProt P25006
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