MolNFT v1 · #129278 · protein
Cu nitrite reductase serial data at varying temperatures rt 0.15MGY
5OFH · Copper-containing nitrite reductase: “Cu nitrite reductase serial data at varying temperatures rt 0.15MGY”. X-ray diffraction, 2 ligands (CU, NO2), 1 pocket (best druggability 0.74). MolNFT v1 #129278 on GenesisL1: 3D structure…
- PDB
- 5OFH
- Type
- protein
- Length
- 332 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper-containing nitrite reductase
- EC
- 1.7.2.1
- UniProt
- P25006
- Ligands
- CU, NO2
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper-containing nitrite reductase (EC 1.7.2.1) | protein | 332 | 11% helix, 41% strand | P25006 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 copies · chains A
- NO2 · Nitrite ion · ion · 5 copies · chains A
- ACT · Acetate ion · additive · 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 | 95 | 0.74 | 0.95 | 20 | empty |
Compared structures
- 5OFH · Cu nitrite reductase serial data at varying temperatures RT 0.15MGy · 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 5OFH · PDBe 5OFH · UniProt P25006
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