Research workbench
Crystal structure of aquifex aeolicus NADH-quinone oxidoreductase subunits nuoe and nuof bound to NADH under anaerobic conditions
Analyse Crystal structure of aquifex aeolicus NADH-quinone oxidoreductase subunits nuoe… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Q9C
- Type
- protein
- Length
- 1,146 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O66842, O66841
- Ligands
- FES, SF4, FMN, NAI, NA, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 155 | — | O66842 |
| B, D | — | protein | 418 | — | O66841 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, C
- SF4 · Iron/sulfur cluster · ligand · 2 copies · chains B, D
- FMN · Flavin mononucleotide · ligand · 2 copies · chains B, D
- NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · 2 copies · chains B, D
- NA · Sodium ion · metal · 5 copies · chains B, D
- SO4 · Sulfate ion · ion · 5 copies · chains A, C, D
- GOL · Glycerol · additive · 5 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6Q9C · Crystal structure of Aquifex aeolicus NADH-qui oxidoreductase subunits NuoE and NuoF… · the same entry in another collection · chain A against A, TM-score 1.00
- O66841 · AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit F (O66841) · a predicted model of the same protein · chain B against A, TM-score 1.00
- O66842 · AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit E (O66842) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O66842
- Every structure of UniProt O66841
- Elsewhere: RCSB PDB 6Q9C · PDBe 6Q9C · UniProt O66842 · UniProt O66841
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