Research workbench
Structure of phosphotriesterase mutant H257Y/L303T
Analyse Structure of phosphotriesterase mutant H257Y/L303T in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OB3
- Type
- protein
- Length
- 660 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
- ZN
- Pockets
- 5 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Parathion hydrolase (EC 3.1.8.1) | protein | 330 | 51% helix, 13% strand | P0A434 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B
- BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B
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 | 216 | 0.67 | 0.85 | 37 | empty |
| 2 | 248 | 0.62 | 0.81 | 35 | empty |
| 3 | 250 | 0.62 | 0.81 | 36 | ZN |
| 4 | 73 | 0.34 | 0.76 | 15 | empty |
| 5 | 61 | 0.34 | 0.77 | 15 | BTB |
Interfaces
1 interface between chains.
- A–B · 1375 Ų buried · 33 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (carboxylation).
Compared structures
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 2OB3 · PDBe 2OB3 · UniProt P0A434
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