Research workbench
Apo form of bacterial arylsulfate sulfotransferase (asst) H436N mutant with mpo in the active site
Analyse Apo form of bacterial arylsulfate sulfotransferase (asst) H436N mutant with mpo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P04
- Type
- protein
- Length
- 1,130 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
- SO4
- Pockets
- 13 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arylsulfate sulfotransferase asst (EC 2.8.2.22) | protein | 567 | 6% helix, 40% strand | E2QE64 |
| B | Arylsulfate sulfotransferase asst (EC 2.8.2.22) | protein | 563 | 6% helix, 40% strand | E2QE64 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains B
- MPO · 3[N-morpholino]propane sulfonic acid · additive · 2 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 | 1123 | 0.71 | 0.75 | 113 | empty |
| 2 | 407 | 0.69 | 0.81 | 54 | MPO |
| 3 | 256 | 0.63 | 0.81 | 21 | empty |
| 4 | 240 | 0.61 | 0.81 | 25 | empty |
| 5 | 289 | 0.61 | 0.79 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 1734 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4P04 · Apo form of bacterial arylsulfate sulfotransferase (ASST) H436N mutant with MPO in the… · 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 4P04 · PDBe 4P04 · UniProt E2QE64
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