Research workbench
Phosphotriesterase PTE_A53_4
Analyse Phosphotriesterase PTE_A53_4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FQE
- Type
- protein
- Length
- 667 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Parathion hydrolase
- EC
- 3.1.8.1
- UniProt
- P0A434
- Ligands
- D6K, ZN
- Pockets
- 5 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Parathion hydrolase (EC 3.1.8.1) | protein | 327 | 52% helix, 14% strand | P0A434 |
| B | Parathion hydrolase (EC 3.1.8.1) | protein | 340 | 51% helix, 14% strand | P0A434 |
Ligands and binding sites
- D6K · (4~{S},6~{R})-2,2,6-trimethyl-1,3-dioxan-4-ol · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 4 copies · chains A, B
- FMT · Formic acid · additive · 2 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 285 | 0.66 | 0.82 | 37 | ZN, D6K |
| 2 | 294 | 0.66 | 0.82 | 37 | FMT, ZN, D6K |
| 3 | 204 | 0.63 | 0.84 | 38 | empty |
| 4 | 64 | 0.34 | 0.77 | 15 | empty |
| 5 | 67 | 0.33 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1482 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (additive adduct).
Compared structures
- 6FQE · Phosphotriesterase PTE_A53_4 · 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 P0A434
- Elsewhere: RCSB PDB 6FQE · PDBe 6FQE · UniProt P0A434
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