MolNFT v1 · #102904 · protein
Bacterial arylsulfate sulfotransferase (asst) H436N mutant with 4- methylumbelliferyl sulfate (mus) in the active site
4P06 · Arylsulfate sulfotransferase asst: “Bacterial arylsulfate sulfotransferase (asst) H436N mutant with 4- methylumbelliferyl sulfate (mus) in the…”. X-ray diffraction, 2 ligands (MUX, SO4), 13 pockets (best druggability 0.71). MolNFT…
- PDB
- 4P06
- Type
- protein
- Length
- 1,128 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arylsulfate sulfotransferase asst
- EC
- 2.8.2.22
- UniProt
- E2QE64
- Ligands
- MUX, SO4
- Pockets
- 13 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Arylsulfate sulfotransferase asst (EC 2.8.2.22) | protein | 564 | 6% helix, 40% strand | E2QE64 |
Ligands and binding sites
- MUX · (4-methyl-2-oxidanylidene-chromen-7-yl) hydrogen sulfate · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1077 | 0.71 | 0.75 | 114 | SO4 |
| 2 | 284 | 0.64 | 0.81 | 29 | empty |
| 3 | 388 | 0.63 | 0.78 | 42 | MUX |
| 4 | 398 | 0.61 | 0.77 | 41 | MUX |
| 5 | 242 | 0.59 | 0.80 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1734 Ų buried · 36 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4P06 · Bacterial arylsulfate sulfotransferase (ASST) H436N mutant with 4-methylumbelliferyl… · the same entry in another collection · 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 E2QE64
- Elsewhere: RCSB PDB 4P06 · PDBe 4P06 · UniProt E2QE64
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