Research workbench
Human SULT1A1 complexed with pap and estradiol
Analyse Human SULT1A1 complexed with pap and estradiol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2D06
- 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
- A3P, EST
- Pockets
- 2 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sulfotransferase 1A1 (EC 2.8.2.1) | protein | 288 | 45% helix, 11% strand | P50225 |
Ligands and binding sites
- A3P · Adenosine-3'-5'-diphosphate · ligand · 2 copies · chains A, B
- EST · Estradiol · 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 | 428 | 0.86 | 0.94 | 61 | A3P, EST |
| 2 | 421 | 0.86 | 0.93 | 59 | A3P, EST |
Interfaces
1 interface between chains.
- A–B · 381 Ų buried · 8 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 P50225
- Elsewhere: RCSB PDB 2D06 · PDBe 2D06 · UniProt P50225
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