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Influenza a nucleoprotein docked into 3D helical structure of the wild type ribonucleoprotein complex obtained using cryoem. conformation 2.

Analyse Influenza a nucleoprotein docked into 3D helical structure of the wild type… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6I54
Type: protein
Length: 802 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleoprotein; Influenza virus nucleoprotein
UniProt: Q1K9H2
Pockets: 13 · best druggability 0.44

Structure

electron microscopy · 2 distinct chains · 45% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Nucleoprotein	protein	382	47% helix, 8% strand	Q1K9H2
B, D	Influenza virus nucleoprotein	protein	19	0% helix, 16% strand	—

Pockets

13 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	121	0.44	0.77	24	empty
2	102	0.43	0.77	19	empty
3	76	0.43	0.80	20	empty
4	123	0.42	0.76	28	empty
5	98	0.38	0.75	20	empty

Interfaces

2 interfaces between chains.

A–B · 1593 Å² buried · 30 hydrogen bonds · protein-protein
C–D · 1592 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

6I54 · Influenza A nucleoprotein docked into 3D helical structure of the wild type… · 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 Q1K9H2
Elsewhere: RCSB PDB 6I54 · PDBe 6I54 · UniProt Q1K9H2

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