Research workbench
Crystal structure of human estrogen sulfotransferase V269E mutant in the presence of paps
Analyse Crystal structure of human estrogen sulfotransferase V269E mutant in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HY3
- Type
- protein
- Length
- 575 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen sulfotransferase
- EC
- 2.8.2.4
- UniProt
- P49888
- Ligands
- PPS
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen sulfotransferase (EC 2.8.2.4) | protein | 287 | 47% helix, 13% strand | P49888 |
| B | Estrogen sulfotransferase (EC 2.8.2.4) | protein | 288 | 47% helix, 13% strand | P49888 |
Ligands and binding sites
- PPS · 3'-phosphate-adenosine-5'-phosphate sulfate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 438 | 0.82 | 0.89 | 49 | PPS |
| 2 | 438 | 0.81 | 0.89 | 54 | PPS |
Interfaces
1 interface between chains.
- A–B · 324 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1HY3 · Crystal structure of human estrogen sulfotransferase V269E mutant in the presence of paps · the same entry in another collection · chain A against A, TM-score 1.00
- P49888 · AlphaFold monomer V2.0 prediction for sulfotransferase 1E1 (P49888) · a predicted model of the same protein · chain B 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 P49888
- Elsewhere: RCSB PDB 1HY3 · PDBe 1HY3 · UniProt P49888
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