Research workbench
Estrogen sulfotransferase with pap
Analyse Estrogen sulfotransferase with pap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AQY
- Type
- protein
- Length
- 563 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen sulfotransferase
- EC
- 2.8.2.4
- UniProt
- P49891
- Ligands
- A3P
- Pockets
- 6 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen sulfotransferase (EC 2.8.2.4) | protein | 283 | 45% helix, 12% strand | P49891 |
| B | Estrogen sulfotransferase (EC 2.8.2.4) | protein | 280 | 45% helix, 13% strand | P49891 |
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
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 571 | 0.87 | 0.92 | 69 | A3P |
| 2 | 527 | 0.87 | 0.93 | 67 | A3P |
| 3 | 150 | 0.40 | 0.74 | 22 | empty |
| 4 | 87 | 0.38 | 0.76 | 16 | empty |
| 5 | 110 | 0.37 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 788 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 P49891
- Elsewhere: RCSB PDB 1AQY · PDBe 1AQY · UniProt P49891
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