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
- 6FU0
- Type
- protein
- Length
- 1,308 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Parathion hydrolase
- EC
- 3.1.8.1
- UniProt
- P0A434
- Ligands
- ZN
- Pockets
- 12 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Parathion hydrolase (EC 3.1.8.1) | protein | 328 | 51% helix, 16% strand | P0A434 |
| B, C | Parathion hydrolase (EC 3.1.8.1) | protein | 327 | 51% helix, 15% strand | P0A434 |
| D | Parathion hydrolase (EC 3.1.8.1) | protein | 326 | 51% helix, 15% strand | P0A434 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, B, C, D
- FMT · Formic acid · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.74 | 0.90 | 30 | empty |
| 2 | 487 | 0.68 | 0.79 | 72 | empty |
| 3 | 303 | 0.66 | 0.82 | 33 | ZN |
| 4 | 231 | 0.63 | 0.82 | 32 | ZN |
| 5 | 266 | 0.63 | 0.81 | 33 | FMT, ZN |
Interfaces
3 interfaces between chains.
- A–B · 1417 Ų buried · 31 hydrogen bonds · protein-protein
- C–D · 1390 Ų buried · 31 hydrogen bonds · protein-protein
- A–C · 407 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent (additive adduct).
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 6FU0 · PDBe 6FU0 · UniProt P0A434
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