Research workbench
Bat influenza a polymerase stuttering complex using 44-mer vrna template with intact OLIGO(U) sequence
Analyse Bat influenza a polymerase stuttering complex using 44-mer vrna template with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T0S
- Type
- protein + RNA
- Length
- 1,743 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- H6QM92, H6QM91, H6QM90
- Ligands
- MG
Structure
electron microscopy · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 708 | — | H6QM92 |
| B | — | protein | 743 | — | H6QM91 |
| C | — | protein | 249 | — | H6QM90 |
| V | — | rna | 33 | — | — |
| M | — | rna | 10 | — | — |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains B, M
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6T0S · Bat Influenza A polymerase stuttering complex using 44-mer vRNA template with intact… · 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 H6QM92
- Every structure of UniProt H6QM91
- Every structure of UniProt H6QM90
- Elsewhere: RCSB PDB 6T0S · PDBe 6T0S · UniProt H6QM92 · UniProt H6QM91 · UniProt H6QM90
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