Research workbench
Human SULT1A1 complexed with pap and P-nitrophenol
Analyse Human SULT1A1 complexed with pap and P-nitrophenol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LS6
- Type
- protein
- Length
- 288 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aryl sulfotransferase
- EC
- 2.8.2.1
- UniProt
- P50225
- Ligands
- NPO, A3P
- Pockets
- 1 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aryl sulfotransferase (EC 2.8.2.1) | protein | 288 | 44% helix, 11% strand | P50225 |
Ligands and binding sites
- NPO · P-nitrophenol · ligand · 2 copies · chains A
- A3P · Adenosine-3'-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 331 | 0.83 | 0.92 | 51 | A3P, NPO |
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 P50225
- Elsewhere: RCSB PDB 1LS6 · PDBe 1LS6 · UniProt P50225
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