MolNFT v1 · #71131 · protein
Structural characterization of the subunit a mutant P235A of the a-ATP synthase
3M4Y · V-type ATP synthase alpha chain: “Structural characterization of the subunit a mutant P235A of the a-ATP synthase”. X-ray diffraction, 7 pockets (best druggability 0.80). MolNFT v1 #71131 on GenesisL1: 3D structure, binding sites…
- PDB
- 3M4Y
- Type
- protein
- Length
- 558 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
- 7 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type ATP synthase alpha chain (EC 3.6.3.14) | protein | 558 | 33% helix, 19% strand | O57728 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 4 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1082 | 0.80 | 0.81 | 117 | empty |
| 2 | 153 | 0.66 | 0.87 | 24 | empty |
| 3 | 232 | 0.53 | 0.77 | 23 | empty |
| 4 | 55 | 0.49 | 0.86 | 16 | empty |
| 5 | 67 | 0.32 | 0.75 | 18 | empty |
Compared structures
- 3M4Y · Structural characterization of the subunit A mutant P235A of the A-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 0.92
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 3M4Y · PDBe 3M4Y · UniProt O57728
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