Research workbench
Cryo-EM structure of tetrahymena thermophila mitochondrial ATP synthase - fo-wing region
Analyse Cryo-EM structure of tetrahymena thermophila mitochondrial ATP synthase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YNV
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- I7LVQ8
- Ligands
- NAD
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| e | — | protein | 417 | — | I7LVQ8 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains e
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6YNV · Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - Fo-wing region · the same entry in another collection · chain e against e, 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 I7LVQ8
- Elsewhere: RCSB PDB 6YNV · PDBe 6YNV · UniProt I7LVQ8
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