Research workbench
Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of DHEA and PAP
Analyse Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q22
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.5
- Source
- Homo sapiens
- Molecule
- sulfotransferase family, cytosolic, 2B, member 1 isoform b
- UniProt
- O00204
- Ligands
- A3P, AND, NA
- Pockets
- 2 · best druggability 0.81
Structure
x-ray diffraction · resolution 2.5 · 1 distinct chain · 45% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | sulfotransferase family, cytosolic, 2B, member 1 isoform b | protein | 291 | 45% helix, 12% strand | O00204 |
Ligands and binding sites
- A3P · Adenosine-3'-5'-diphosphate · ligand · chains A
- AND · 3-beta-hydroxy-5-androsten-17-one · ligand · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 480 | 0.81 | 0.88 | 50 | A3P, AND |
| 2 | 71 | 0.33 | 0.75 | 14 | empty |
Compared structures
- 1Q22 · Crystal structure of human cholesterol sulfotransferase (SULT2B1B) in the presence of… · the same entry in another collection · chain A against A, TM-score 1.00
- O00204 · AlphaFold monomer V2.0 prediction for sulfotransferase 2B1 (O00204) · a predicted model of the same protein · 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 O00204
- Elsewhere: RCSB PDB 1Q22 · PDBe 1Q22 · UniProt O00204
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