Research workbench
Crystal structure of mouse cytosolic sulfotransferase MSULT3A1
Analyse Crystal structure of mouse cytosolic sulfotransferase MSULT3A1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7V1O
- Type
- protein
- Length
- 574 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amine sulfotransferase
- EC
- 2.8.2.3
- UniProt
- O35403
- Ligands
- 5I2, A3P
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amine sulfotransferase (EC 2.8.2.3) | protein | 288 | 45% helix, 11% strand | O35403 |
| B | Amine sulfotransferase (EC 2.8.2.3) | protein | 286 | 45% helix, 11% strand | O35403 |
Ligands and binding sites
- 5I2 · naphthalen-1-amine · ligand · 2 copies · chains A, B
- A3P · Adenosine-3'-5'-diphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 309 | 0.84 | 0.94 | 49 | 5I2, A3P |
| 2 | 305 | 0.84 | 0.94 | 50 | 5I2, A3P |
| 3 | 442 | 0.76 | 0.85 | 55 | empty |
| 4 | 212 | 0.61 | 0.82 | 24 | empty |
| 5 | 63 | 0.47 | 0.84 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 594 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
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 O35403
- Elsewhere: RCSB PDB 7V1O · PDBe 7V1O · UniProt O35403
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