Research workbench
Large C-terminal domain of influenza a virus RNA-dependent polymerase PB2
Analyse Large C-terminal domain of influenza a virus RNA-dependent polymerase PB2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CW4
- Type
- protein
- Length
- 208 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polymerase basic protein 2
- EC
- 2.7.-.-
- UniProt
- P03428
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polymerase basic protein 2 (EC 2.7.-.-) | protein | 208 | 38% helix, 20% strand | P03428 |
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 | 197 | 0.50 | 0.77 | 28 | empty |
| 2 | 86 | 0.33 | 0.74 | 19 | empty |
Compared structures
- 3CW4 · Large c-terminal domain of influenza a virus RNA-dependent polymerase PB2 · 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 P03428
- Elsewhere: RCSB PDB 3CW4 · PDBe 3CW4 · UniProt P03428
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