Research workbench
Arpte (K185R/D208G/N265D/T274N)
Analyse Arpte (K185R/D208G/N265D/T274N) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A4J
- Type
- protein
- Length
- 328 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphotriesterase
- EC
- 3.1.8.1
- UniProt
- Q93LD7
- Ligands
- CO
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphotriesterase (EC 3.1.8.1) | protein | 328 | 51% helix, 14% strand | Q93LD7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.50 | 0.80 | 27 | EDO |
| 2 | 73 | 0.33 | 0.75 | 17 | empty |
| 3 | 63 | 0.32 | 0.76 | 15 | empty |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 3A4J · arPTE (K185R/D208G/N265D/T274N) · 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 Q93LD7
- Elsewhere: RCSB PDB 3A4J · PDBe 3A4J · UniProt Q93LD7
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