Research workbench
EBV dutpase double mutant GLY78ASP-ASP131SER with dump
Analyse EBV dutpase double mutant GLY78ASP-ASP131SER with dump in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WE2
- Type
- protein
- Length
- 248 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- EC
- 3.6.1.23
- UniProt
- P03195
- Ligands
- UMP, SO4
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Deoxyuridine 5'-triphosphate nucleotidohydrolase (EC 3.6.1.23) | protein | 248 | 4% helix, 50% strand | P03195 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.52 | 0.79 | 20 | UMP |
| 2 | 154 | 0.42 | 0.74 | 30 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2WE2 · EBV dUTPase double mutant Gly78Asp-Asp131Ser with dUMP · 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 P03195
- Elsewhere: RCSB PDB 2WE2 · PDBe 2WE2 · UniProt P03195
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