Research workbench
Sulphotransferase-18 from arabidopsis thaliana in complex with 3'- phosphoadenosine 5'-phosphate (PAP)AND sinigrin
Analyse Sulphotransferase-18 from arabidopsis thaliana in complex with 3'… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MEX
- Type
- protein
- Length
- 322 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytosolic sulfotransferase 18
- EC
- 2.8.2.-
- UniProt
- Q9C9C9
- Ligands
- PAP, SZZ
- Pockets
- 4 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytosolic sulfotransferase 18 (EC 2.8.2.-) | protein | 322 | 49% helix, 11% strand | Q9C9C9 |
Ligands and binding sites
- PAP · 3'-phosphate-adenosine-5'-diphosphate · ligand · chains A
- SZZ · Sinigrin · ligand · chains A
- EDO · 1,2-ethanediol · additive · 10 copies · chains A
- BU2 · 1,3-butanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 512 | 0.83 | 0.89 | 62 | PAP, SZZ, EDO |
| 2 | 51 | 0.43 | 0.83 | 11 | empty |
| 3 | 93 | 0.36 | 0.74 | 20 | EDO |
| 4 | 88 | 0.33 | 0.73 | 19 | EDO |
Compared structures
- 5MEX · Sulphotransferase-18 from Arabidopsis thaliana in complex with 3'-phosphoadenosine… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9C9C9 · AlphaFold monomer V2.0 prediction for cytosolic sulfotransferase 18 (Q9C9C9) · 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 Q9C9C9
- Elsewhere: RCSB PDB 5MEX · PDBe 5MEX · UniProt Q9C9C9
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