Research workbench
Epstein-barr virus alkaline nuclease D203S mutant
Analyse Epstein-barr virus alkaline nuclease D203S mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W4B
- Type
- protein
- Length
- 893 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alkaline exonuclease
- EC
- 3.1.11.-
- UniProt
- P03217
- Pockets
- 14 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alkaline exonuclease (EC 3.1.11.-) | protein | 455 | 41% helix, 17% strand | P03217 |
| B | Alkaline exonuclease (EC 3.1.11.-) | protein | 438 | 41% helix, 18% strand | P03217 |
Pockets
14 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1093 | 0.83 | 0.84 | 96 | empty |
| 2 | 408 | 0.55 | 0.74 | 44 | empty |
| 3 | 317 | 0.52 | 0.74 | 39 | empty |
| 4 | 169 | 0.46 | 0.76 | 26 | empty |
| 5 | 139 | 0.43 | 0.76 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 956 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2W4B · Epstein-Barr virus alkaline nuclease D203S mutant · 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 P03217
- Elsewhere: RCSB PDB 2W4B · PDBe 2W4B · UniProt P03217
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