MolNFT v1 · #56949 · protein
Crystal structure of mouse cytosolic sulfotransferase MSULT1D1 complex with pap and P-nitrophenol
2ZVP · Tyrosine-ester sulfotransferase: “Crystal structure of mouse cytosolic sulfotransferase MSULT1D1 complex with pap and P-nitrophenol”. X-ray diffraction, 2 ligands (NPO, A3P), 1 pocket (best druggability 0.83). MolNFT v1 #56949 on…
- PDB
- 2ZVP
- Type
- protein
- Length
- 289 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-ester sulfotransferase
- EC
- 2.8.2.9
- UniProt
- Q9R2C2
- 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 |
|---|---|---|---|---|---|
| X | Tyrosine-ester sulfotransferase (EC 2.8.2.9) | protein | 289 | 44% helix, 11% strand | Q9R2C2 |
Ligands and binding sites
- NPO · P-nitrophenol · ligand · 2 copies · chains X
- A3P · Adenosine-3'-5'-diphosphate · ligand · chains X
- GOL · Glycerol · additive · chains X
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 | 344 | 0.83 | 0.92 | 57 | A3P, NPO |
Compared structures
- 2ZVP · Crystal structure of mouse cytosolic sulfotransferase mSULT1D1 complex with PAP and… · the same entry in another collection · chain X against X, 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 Q9R2C2
- Elsewhere: RCSB PDB 2ZVP · PDBe 2ZVP · UniProt Q9R2C2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.