Research workbench
Crystal structure of nqrf in hexagonal space group
Analyse Crystal structure of nqrf in hexagonal space group in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UAJ
- Type
- protein
- Length
- 280 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Na(+)-translocating NADH-quinone reductase subunit F
- EC
- 1.6.5.-
- UniProt
- A5F5Y4
- Ligands
- FAD, SO4
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Na(+)-translocating NADH-quinone reductase subunit F (EC 1.6.5.-) | protein | 280 | 30% helix, 31% strand | A5F5Y4 |
Ligands and binding sites
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 | 455 | 0.65 | 0.78 | 60 | FAD, SO4 |
Compared structures
- 4UAJ · Crystal structure of NqrF in hexagonal space group · the same entry in another collection · chain A against A, TM-score 1.00
- A5F5Y4 · AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone reductase subunit… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 A5F5Y4
- Elsewhere: RCSB PDB 4UAJ · PDBe 4UAJ · UniProt A5F5Y4
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