Research workbench
Crystal structure of RNA polymerase PB1-PB2 subunits from influenza a virus
Analyse Crystal structure of RNA polymerase PB1-PB2 subunits from influenza a virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZTT
- Type
- protein
- Length
- 218 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-directed RNA polymerase catalytic subunit; Polymerase basic protein 2
- EC
- 2.7.7.48
- UniProt
- P03431, P03428
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 3 distinct chains · 69% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA-directed RNA polymerase catalytic subunit (EC 2.7.7.48) | protein | 73 | 67% helix, 1% strand | P03431 |
| B, D | Polymerase basic protein 2 | protein | 37 | 76% helix, 3% strand | P03428 |
| C | RNA-directed RNA polymerase catalytic subunit (EC 2.7.7.48) | protein | 71 | 68% helix, 1% strand | P03431 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.34 | 0.74 | 18 | empty |
| 2 | 58 | 0.30 | 0.74 | 11 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1629 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1477 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 253 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 244 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 236 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified (engineered).
Compared structures
- 2ZTT · Crystal Structure of RNA polymerase PB1-PB2 subunits from Influenza A Virus · 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 P03431
- Every structure of UniProt P03428
- Elsewhere: RCSB PDB 2ZTT · PDBe 2ZTT · UniProt P03431 · UniProt P03428
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