MolNFT v1 · #102903 · protein
Bacterial arylsulfate sulfotransferase (asst) H436N mutant with 4- nitrophenyl sulfate (pns) in the active site
4P05 · Arylsulfate sulfotransferase asst: “Bacterial arylsulfate sulfotransferase (asst) H436N mutant with 4- nitrophenyl sulfate (pns) in the active…”. X-ray diffraction, 2 ligands (4NS, SO4), 11 pockets (best druggability 0.71). MolNFT…
- PDB
- 4P05
- 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
- 4NS, SO4
- Pockets
- 11 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Arylsulfate sulfotransferase asst (EC 2.8.2.22) | protein | 564 | 7% helix, 40% strand | E2QE64 |
Ligands and binding sites
- 4NS · 4-nitrophenyl 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
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1132 | 0.71 | 0.75 | 110 | empty |
| 2 | 277 | 0.62 | 0.80 | 30 | empty |
| 3 | 353 | 0.62 | 0.78 | 46 | 4NS |
| 4 | 228 | 0.62 | 0.81 | 23 | empty |
| 5 | 368 | 0.61 | 0.77 | 46 | 4NS |
Interfaces
1 interface between chains.
- A–B · 1717 Ų buried · 34 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4P05 · Bacterial arylsulfate sulfotransferase (ASST) H436N mutant with 4-nitrophenyl sulfate… · 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 4P05 · PDBe 4P05 · UniProt E2QE64
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