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Bat influenza a polymerase termination complex with pyrophosphate using 44-mer vrna template with mutated OLIGO(U) sequence

Analyse Bat influenza a polymerase termination complex with pyrophosphate using 44-mer… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6TW1
Type: protein + RNA
Length: 2,226 residues
Chains: 5
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: H6QM92, H6QM91, H6QM90
Ligands: M4H, POP, MG

Structure

electron microscopy · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	703	—	H6QM92
B	—	protein	740	—	H6QM91
C	—	protein	740	—	H6QM90
V	—	rna	33	—	—
M	—	rna	10	—	—

Ligands and binding sites

M4H · 5-oxidanyl-4-oxidanylidene-1-[(1-pyrrolo[2,3-b]pyridin-1-ylcyclopentyl)methyl]pyridine-3-carboxylic acid · ligand · chains A
POP · Pyrophosphate 2- · ligand · chains B, M
MG · Magnesium ion · metal · 4 copies · chains A, B, M

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6TW1 · Bat Influenza A polymerase termination complex with pyrophosphate using 44-mer vRNA… · 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 6TW1 · PDBe 6TW1 · UniProt H6QM92 · UniProt H6QM91 · UniProt H6QM90

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