Research workbench
Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3-phosphoadenosine 5-phosphate
Analyse Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A3R
- Type
- protein
- Length
- 574 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Monoamine-sulfating phenol sulfotransferase
- EC
- 2.8.2.1
- UniProt
- P50224
- Ligands
- A3P, LDP
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Monoamine-sulfating phenol sulfotransferase (EC 2.8.2.1) | protein | 287 | 45% helix, 11% strand | P50224 |
Ligands and binding sites
- A3P · Adenosine-3'-5'-diphosphate · ligand · 2 copies · chains A, B
- LDP · L-dopamine · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 370 | 0.84 | 0.93 | 56 | A3P, LDP |
| 2 | 358 | 0.83 | 0.92 | 55 | A3P, LDP |
| 3 | 384 | 0.59 | 0.76 | 39 | empty |
| 4 | 109 | 0.40 | 0.76 | 16 | empty |
| 5 | 54 | 0.36 | 0.79 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 249 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2A3R · Crystal Structure of Human Sulfotransferase SULT1A3 in Complex with Dopamine and… · the same entry in another collection · 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 P50224
- Elsewhere: RCSB PDB 2A3R · PDBe 2A3R · UniProt P50224
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