Research workbench
Crystal structure of human sulfotransferase SULT1C1 in complex with pap
Analyse Crystal structure of human sulfotransferase SULT1C1 in complex with pap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BFX
- Type
- protein
- Length
- 501 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfotransferase 1C2
- EC
- 2.8.2.-
- UniProt
- O00338
- Ligands
- A3P
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfotransferase 1C2 (EC 2.8.2.-) | protein | 253 | 47% helix, 11% strand | O00338 |
| B | Sulfotransferase 1C2 (EC 2.8.2.-) | protein | 248 | 46% helix, 11% strand | O00338 |
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
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 342 | 0.74 | 0.85 | 41 | A3P |
| 2 | 357 | 0.70 | 0.82 | 51 | A3P |
| 3 | 263 | 0.69 | 0.84 | 33 | empty |
| 4 | 110 | 0.53 | 0.82 | 22 | empty |
| 5 | 59 | 0.30 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 502 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 3BFX · Crystal structure of human sulfotransferase SULT1C1 in complex with PAP · the same entry in another collection · chain A against A, TM-score 1.00
- O00338 · AlphaFold monomer V2.0 prediction for sulfotransferase 1C2 (O00338) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 O00338
- Elsewhere: RCSB PDB 3BFX · PDBe 3BFX · UniProt O00338
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