Research workbench
The structure of the ATP sulfurylase from allochromatium vinosum in the open state
Analyse The structure of the ATP sulfurylase from allochromatium vinosum in the open… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DNX
- Type
- protein
- Length
- 792 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfate adenylyltransferase
- EC
- 2.7.7.4
- UniProt
- O66036
- Pockets
- 9 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sulfate adenylyltransferase (EC 2.7.7.4) | protein | 396 | 38% helix, 19% strand | O66036 |
Ligands and binding sites
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 657 | 0.74 | 0.80 | 54 | empty |
| 2 | 544 | 0.68 | 0.78 | 52 | empty |
| 3 | 459 | 0.64 | 0.77 | 46 | empty |
| 4 | 278 | 0.64 | 0.81 | 45 | empty |
| 5 | 412 | 0.60 | 0.76 | 41 | MES |
Interfaces
1 interface between chains.
- A–B · 1836 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 4DNX · The structure of the ATP sulfurylase from Allochromatium vinosum in the open state · the same entry in another collection · chain A against A, TM-score 1.00
- O66036 · AlphaFold monomer V2.0 prediction for sulfate adenylyltransferase (O66036) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 O66036
- Elsewhere: RCSB PDB 4DNX · PDBe 4DNX · UniProt O66036
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