Research workbench
Phosphotriesterase variant R2
Analyse Phosphotriesterase variant R2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XD5
- Type
- protein
- Length
- 660 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphotriesterase variant pte-R2
- UniProt
- A0A060GSW5
- Ligands
- ZN
- Pockets
- 6 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphotriesterase variant pte-R2 | protein | 331 | 50% helix, 15% strand | A0A060GSW5 |
| G | Phosphotriesterase variant pte-R2 | protein | 329 | 51% helix, 15% strand | A0A060GSW5 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, G
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A, G
- CAC · Cacodylate ion · additive · 2 copies · chains A, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.67 | 0.87 | 38 | empty |
| 2 | 251 | 0.57 | 0.78 | 35 | CAC |
| 3 | 217 | 0.54 | 0.78 | 31 | CAC |
| 4 | 82 | 0.38 | 0.77 | 20 | empty |
| 5 | 70 | 0.32 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–G · 1357 Ų buried · 35 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (carboxylation).
Compared structures
- 4XD5 · Phosphotriesterase variant R2 · 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 A0A060GSW5
- Elsewhere: RCSB PDB 4XD5 · PDBe 4XD5 · UniProt A0A060GSW5
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