Research workbench
Crystal structure of 7-alpha-hydroxyl bile acid sulfotransferase (SULT2A8)
Analyse Crystal structure of 7-alpha-hydroxyl bile acid sulfotransferase (SULT2A8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7D1X
- Type
- protein
- Length
- 523 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfotransferase
- EC
- 2.8.2.-
- UniProt
- Q8BGL3
- Ligands
- CHD, A3P
- Pockets
- 8 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfotransferase (EC 2.8.2.-) | protein | 272 | 45% helix, 10% strand | Q8BGL3 |
| B | Sulfotransferase (EC 2.8.2.-) | protein | 251 | 48% helix, 10% strand | Q8BGL3 |
Ligands and binding sites
- CHD · Cholic acid · 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
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 612 | 0.82 | 0.87 | 64 | CHD |
| 2 | 419 | 0.78 | 0.86 | 50 | CHD, A3P |
| 3 | 108 | 0.72 | 0.92 | 18 | empty |
| 4 | 159 | 0.71 | 0.89 | 27 | A3P |
| 5 | 72 | 0.50 | 0.84 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 509 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 7D1X · Crystal structure of 7-alpha-hydroxyl bile acid sulfotransferase (Sult2a8) · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8BGL3
- Elsewhere: RCSB PDB 7D1X · PDBe 7D1X · UniProt Q8BGL3
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