MolNFT v1 · #52941 · protein

Fitting of influenza virus np structure into the 9-fold symmetryzed cryoem reconstruction of an active rnp particle.

2WFS · Nucleoprotein: “Fitting of influenza virus np structure into the 9-fold symmetryzed cryoem reconstruction of an active rnp…”. Electron microscopy, 20 pockets (best druggability 0.78). MolNFT v1 #52941 on GenesisL1: 3D structure…

PDB: 2WFS
Type: protein
Length: 3,834 residues
Chains: 9
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleoprotein
Pockets: 20 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 46% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I	Nucleoprotein	protein	426	46% helix, 9% strand	—

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	999	0.78	0.81	144	empty
2	1042	0.77	0.80	160	empty
3	1110	0.77	0.80	154	empty
4	978	0.77	0.80	146	empty
5	934	0.77	0.81	132	empty

Interfaces

9 interfaces between chains.

A–B · 551 Å² buried · 10 hydrogen bonds · protein-protein
E–F · 549 Å² buried · 10 hydrogen bonds · protein-protein
D–E · 549 Å² buried · 10 hydrogen bonds · protein-protein
B–C · 549 Å² buried · 10 hydrogen bonds · protein-protein
H–I · 548 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

2WFS · Fitting of influenza virus NP structure into the 9-fold symmetryzed cryoEM reconstruction… · 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
Elsewhere: RCSB PDB 2WFS · PDBe 2WFS

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