MolNFT v1 · #156258 · protein
V/A-ATPase from thermus thermophilus, the soluble domain, including V1, D, two eg stalks, and N-terminal domain of a-subunit.
6LY8: “V/A-ATPase from thermus thermophilus, the soluble domain, including V1, D, two eg stalks, and N-terminal…”. Electron microscopy, 1 ligand (ADP). MolNFT v1 #156258 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6LY8
- Type
- protein
- Length
- 3,418 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q56403, Q56404, O87880, P74903
- Ligands
- ADP
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 577 | — | Q56403 |
| D, E, F | — | protein | 459 | — | Q56404 |
| G | — | protein | 210 | — | O87880 |
| H | — | protein | 100 | — | P74903 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6LY8 · V/A-ATPase from Thermus thermophilus, the soluble domain, including V1, d, two EG stalks… · the same entry in another collection · chain H against H, TM-score 1.00
- Q56404 · AlphaFold monomer V2.0 prediction for V-type ATP synthase beta chain (Q56404) · a predicted model of the same protein · chain D against A, TM-score 0.97
- Q56403 · AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (Q56403) · a predicted model of the same protein · chain A against A, TM-score 0.96
- O87880 · AlphaFold monomer V2.0 prediction for V-type ATP synthase subunit D (O87880) · a predicted model of the same protein · chain G against A, TM-score 0.85
- P74903 · AlphaFold monomer V2.0 prediction for V-type ATP synthase subunit F (P74903) · a predicted model of the same protein · chain H against A, TM-score 0.68
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 Q56403
- Every structure of UniProt Q56404
- Every structure of UniProt O87880
- Every structure of UniProt P74903
- Elsewhere: RCSB PDB 6LY8 · PDBe 6LY8 · UniProt Q56403 · UniProt Q56404 · UniProt O87880 · UniProt P74903
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