Research workbench
A mechanism for the activation of the influenza virus transcriptase
Analyse A mechanism for the activation of the influenza virus transcriptase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F5P
- Type
- protein
- Length
- 4,411 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9IMP5, Q9IMP4, Q9IMP3
- Ligands
- MG
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 708 | — | Q9IMP5 |
| B | — | protein | 710 | — | Q9IMP4 |
| C | — | protein | 721 | — | Q9IMP4 |
| E, F | — | protein | 771 | — | Q9IMP3 |
| G | — | protein | 12 | — | — |
| H | — | protein | 10 | — | — |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6F5P · A mechanism for the activation of the influenza virus transcriptase · 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 Q9IMP5
- Every structure of UniProt Q9IMP4
- Every structure of UniProt Q9IMP3
- Elsewhere: RCSB PDB 6F5P · PDBe 6F5P · UniProt Q9IMP5 · UniProt Q9IMP4 · UniProt Q9IMP3
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