MolNFT v1 · #161822 · protein
Cryo-EM structure of dimeric quinol dependent nitric oxide reductase (qnor) VAL495ALA mutant from alcaligenes xylosoxidans
6QQ6: “Cryo-EM structure of dimeric quinol dependent nitric oxide reductase (qnor) VAL495ALA mutant from alcaligenes…”. Electron microscopy, 4 ligands (HEM, LOP, FE). MolNFT v1 #161822 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6QQ6
- Type
- protein
- Length
- 1,486 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0D6H8R3
- Ligands
- HEM, LOP, FE, CA
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 743 | — | A0A0D6H8R3 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B
- LOP · (1R)-2-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(dodecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate · ligand · 3 copies · chains A, B
- FE · Fe (III) ion · metal · 2 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
- LMT · Dodecyl-beta-D-maltoside · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6QQ6 · Cryo-EM structure of dimeric quinol dependent nitric oxide reductase (qNOR) Val495Ala… · 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 A0A0D6H8R3
- Elsewhere: RCSB PDB 6QQ6 · PDBe 6QQ6 · UniProt A0A0D6H8R3
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