MolNFT v2 · #18867 · protein
Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of DHEA and PAP
1Q22 · sulfotransferase family, cytosolic, 2B, member 1 isoform b: “Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of DHEA and PAP”. X-ray diffraction at 2.5, 3 ligands (A3P, AND, NA), 2 pockets (best…
- 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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