MolNFT v1 · #78605 · protein
Structural characterization of the subunit a mutant F427W of the a-ATP synthase from pyrococcus horikoshii
3SDZ · V-type ATP synthase alpha chain: “Structural characterization of the subunit a mutant F427W of the a-ATP synthase from pyrococcus horikoshii”. X-ray diffraction, 3 pockets (best druggability 0.81). MolNFT v1 #78605 on GenesisL1: 3D…
- PDB
- 3SDZ
- Type
- protein
- Length
- 548 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
- Pockets
- 3 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type ATP synthase alpha chain (EC 3.6.3.14) | protein | 548 | 32% helix, 19% strand | O57728 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 6 copies · chains A
- ACY · Acetic acid · additive · 6 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1005 | 0.81 | 0.82 | 103 | MPD |
| 2 | 113 | 0.56 | 0.84 | 22 | ACY |
| 3 | 57 | 0.28 | 0.74 | 13 | empty |
Compared structures
- 3SDZ · Structural characterization of the subunit A mutant F427W 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 3SDZ · PDBe 3SDZ · UniProt O57728
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