Research workbench
Mammalian V-ATPase from rat brain - composite model of rotational state 1 bound to ADP and sidk (built from focused refinement models)
Analyse Mammalian V-ATPase from rat brain - composite model of rotational state 1 bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VQ6
- Type
- protein
- Length
- 8,454 residues
- Chains
- 34
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D4A133, P62815, Q5FVI6, Q6P503, Q6PCU2, P50408, Q8R2H0, Q5ZWW6, P25286, B0K022, O54715, Q5M7T6, Q5EB76, D3ZIM6, P63081, Q6AXS4
- Ligands
- ADP, MG
Structure
electron microscopy · 18 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 600 | — | D4A133 |
| D, E, F | — | protein | 459 | — | P62815 |
| G | — | protein | 360 | — | Q5FVI6 |
| H | — | protein | 214 | — | Q6P503 |
| I, J, K | — | protein | 225 | — | Q6PCU2 |
| L | — | protein | 110 | — | P50408 |
| M, N, O | — | protein | 114 | — | Q8R2H0 |
| Q | — | protein | 224 | — | Q5ZWW6 |
| R | — | protein | 212 | — | Q5ZWW6 |
| S | — | protein | 232 | — | Q5ZWW6 |
| a | — | protein | 750 | — | P25286 |
| b | — | protein | 203 | — | B0K022 |
| c | — | protein | 41 | — | O54715 |
| d | — | protein | 350 | — | Q5M7T6 |
| e | — | protein | 78 | — | Q5EB76 |
| f | — | protein | 84 | — | D3ZIM6 |
| g, h, i, j, k, l, m, n, o | — | protein | 150 | — | P63081 |
| p | — | protein | 52 | — | Q6AXS4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VQ6 · Mammalian V-ATPase from rat brain - composite model of rotational state 1 bound to ADP… · the same entry in another collection · chain K against K, 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 D4A133
- Every structure of UniProt P62815
- Every structure of UniProt Q5FVI6
- Every structure of UniProt Q6P503
- Every structure of UniProt Q6PCU2
- Every structure of UniProt P50408
- Every structure of UniProt Q8R2H0
- Every structure of UniProt Q5ZWW6
- Every structure of UniProt P25286
- Every structure of UniProt B0K022
- Every structure of UniProt O54715
- Every structure of UniProt Q5M7T6
- Every structure of UniProt Q5EB76
- Every structure of UniProt D3ZIM6
- Every structure of UniProt P63081
- Every structure of UniProt Q6AXS4
- Elsewhere: RCSB PDB 6VQ6 · PDBe 6VQ6 · UniProt D4A133 · UniProt P62815 · UniProt Q5FVI6 · UniProt Q6P503 · UniProt Q6PCU2 · UniProt P50408 · UniProt Q8R2H0 · UniProt Q5ZWW6 · UniProt P25286 · UniProt B0K022 · UniProt O54715 · UniProt Q5M7T6 · UniProt Q5EB76 · UniProt D3ZIM6 · UniProt P63081 · UniProt Q6AXS4
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