MolNFT v1 · #155266 · protein
Quinol-dependent nitric oxide reductase (qnor) from neisseria meningitidis in the monomeric oxidized state with zinc complex.
6L1X · Nitric-oxide reductase: “Quinol-dependent nitric oxide reductase (qnor) from neisseria meningitidis in the monomeric oxidized state…”. X-ray diffraction, 4 ligands (HEM, ZN, FE), 6 pockets (best druggability 0.88). MolNFT v1 #155266…
- PDB
- 6L1X
- Type
- protein
- Length
- 708 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitric-oxide reductase
- EC
- 1.7.99.7
- UniProt
- C6S880
- Ligands
- HEM, ZN, FE, CA
- Pockets
- 6 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 68% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitric-oxide reductase (EC 1.7.99.7) | protein | 708 | 68% helix, 2% strand | C6S880 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A
- ZN · Zinc ion · metal · 3 copies · chains A
- FE · Fe (III) ion · metal · chains A
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 804 | 0.88 | 0.91 | 87 | HEM |
| 2 | 837 | 0.79 | 0.81 | 60 | empty |
| 3 | 213 | 0.68 | 0.85 | 22 | empty |
| 4 | 89 | 0.46 | 0.79 | 16 | empty |
| 5 | 58 | 0.45 | 0.83 | 20 | empty |
Modifications
Observed in the structure: 1 cofactor (heme attachment).
Compared structures
- 6L1X · Quinol-dependent nitric oxide reductase (qNOR) from Neisseria meningitidis in the… · the same entry in another collection · 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 C6S880
- Elsewhere: RCSB PDB 6L1X · PDBe 6L1X · UniProt C6S880
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