Research workbench
Crystal structure of ancestral variant B9 of sult 1A1 in complex with pap and P-nitrophenol
Analyse Crystal structure of ancestral variant B9 of sult 1A1 in complex with pap and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QVU
- Type
- protein
- Length
- 576 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfotransferase 1A1
- EC
- 2.8.2.1
- UniProt
- P50225
- Ligands
- NPO, A3P
- Pockets
- 5 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sulfotransferase 1A1 (EC 2.8.2.1) | protein | 288 | 42% helix, 11% strand | P50225 |
Ligands and binding sites
- NPO · P-nitrophenol · ligand · 2 copies · chains A, B
- A3P · Adenosine-3'-5'-diphosphate · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 313 | 0.85 | 0.94 | 57 | NPO, A3P |
| 2 | 306 | 0.84 | 0.94 | 61 | A3P, NPO |
| 3 | 69 | 0.49 | 0.84 | 18 | empty |
| 4 | 56 | 0.34 | 0.78 | 15 | empty |
| 5 | 50 | 0.29 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 291 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3QVU · Crystal structure of Ancestral variant b9 of SULT 1A1 in complex with PAP and… · the same entry in another collection · chain A against A, TM-score 1.00
- P50225 · AlphaFold monomer V2.0 prediction for sulfotransferase 1A1 (P50225) · 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 P50225
- Elsewhere: RCSB PDB 3QVU · PDBe 3QVU · UniProt P50225
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