Research workbench
Crystal structure of the human hydroxysteroid sulfotransferase in the presence of pap
Analyse Crystal structure of the human hydroxysteroid sulfotransferase in the presence… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EFH
- Type
- protein
- Length
- 563 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hydroxysteroid sulfotransferase
- EC
- 2.8.2.2
- UniProt
- Q06520
- Ligands
- A3P
- Pockets
- 4 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hydroxysteroid sulfotransferase (EC 2.8.2.2) | protein | 281 | 48% helix, 11% strand | Q06520 |
| B | Hydroxysteroid sulfotransferase (EC 2.8.2.2) | protein | 282 | 48% helix, 11% strand | Q06520 |
Ligands and binding sites
- 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
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1137 | 0.88 | 0.88 | 144 | A3P |
| 2 | 313 | 0.67 | 0.81 | 38 | empty |
| 3 | 165 | 0.52 | 0.79 | 28 | empty |
| 4 | 55 | 0.31 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 903 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1EFH · Crystal structure of the human hydroxysteroid sulfotransferase in the presence of pap · the same entry in another collection · chain A against A, TM-score 1.00
- Q06520 · AlphaFold monomer V2.0 prediction for sulfotransferase 2A1 (Q06520) · 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 Q06520
- Elsewhere: RCSB PDB 1EFH · PDBe 1EFH · UniProt Q06520
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