Research workbench
Crystal structure of ATP synthase subunit alpha (TM1612) from thermotoga maritima at 2.10 a resolution
Analyse Crystal structure of ATP synthase subunit alpha (TM1612) from thermotoga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R9V
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase subunit alpha
- EC
- 3.6.3.14
- UniProt
- Q9X1U7
- Ligands
- ATP, MG, CL
- Pockets
- 5 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP synthase subunit alpha (EC 3.6.3.14) | protein | 487 | 40% helix, 21% strand | Q9X1U7 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · chains A
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 270 | 0.60 | 0.79 | 31 | MG, ATP |
| 2 | 109 | 0.45 | 0.79 | 21 | empty |
| 3 | 53 | 0.36 | 0.79 | 15 | empty |
| 4 | 79 | 0.33 | 0.74 | 13 | empty |
| 5 | 81 | 0.31 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 2R9V · Crystal structure of ATP synthase subunit alpha (TM1612) from Thermotoga maritima at 2.10… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X1U7 · AlphaFold monomer V2.0 prediction for ATP synthase subunit alpha (Q9X1U7) · 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 Q9X1U7
- Elsewhere: RCSB PDB 2R9V · PDBe 2R9V · UniProt Q9X1U7
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