Research workbench
Crystal structure of vanadate bound subunit a of the A1AO ATP synthase
Analyse Crystal structure of vanadate bound subunit a of the A1AO ATP synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P20
- Type
- protein
- Length
- 517 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- V-type ATP synthase alpha chain
- EC
- 3.6.3.14
- UniProt
- O57728
- Ligands
- VO4
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type ATP synthase alpha chain (EC 3.6.3.14) | protein | 517 | 34% helix, 19% strand | O57728 |
Ligands and binding sites
- VO4 · Vanadate ion · ion · 2 copies · chains A
- ACY · Acetic acid · additive · 6 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 729 | 0.75 | 0.81 | 69 | ACY, MPD |
| 2 | 197 | 0.58 | 0.80 | 40 | MPD |
| 3 | 55 | 0.37 | 0.79 | 20 | ACY |
| 4 | 73 | 0.36 | 0.77 | 18 | VO4 |
| 5 | 51 | 0.30 | 0.76 | 19 | empty |
Compared structures
- 3P20 · Crystal structure of vanadate bound subunit A of the A1AO ATP synthase · the same entry in another collection · chain A against A, TM-score 1.00
- O57728 · AlphaFold monomer V2.0 prediction for V-type ATP synthase alpha chain (O57728) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 O57728
- Elsewhere: RCSB PDB 3P20 · PDBe 3P20 · UniProt O57728
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