MolNFT v1 · #78606 · protein
Structural characterization of the subunit a mutant F508W of the a-ATP synthase from pyrococcus horikoshii
3SE0 · V-type ATP synthase alpha chain: “Structural characterization of the subunit a mutant F508W of the a-ATP synthase from pyrococcus horikoshii”. X-ray diffraction, 1 ligand (SO4), 7 pockets (best druggability 0.78). MolNFT v1 #78606…
- PDB
- 3SE0
- Type
- protein
- Length
- 519 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
- SO4
- Pockets
- 7 · best druggability 0.78
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 | 519 | 34% helix, 19% strand | O57728 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A
- ACY · Acetic acid · additive · 2 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
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 762 | 0.78 | 0.82 | 59 | empty |
| 2 | 165 | 0.57 | 0.81 | 28 | empty |
| 3 | 185 | 0.49 | 0.77 | 21 | empty |
| 4 | 90 | 0.42 | 0.78 | 20 | SO4 |
| 5 | 89 | 0.38 | 0.76 | 17 | empty |
Compared structures
- 3SE0 · Structural characterization of the subunit A mutant F508W of the A-ATP synthase from… · 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 0.93
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 3SE0 · PDBe 3SE0 · UniProt O57728
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