Research workbench

Crystal structure of a vesicular stomatitis virus nucleocapsid protein SER290TRP mutant

Analyse Crystal structure of a vesicular stomatitis virus nucleocapsid protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QVJ
Type: protein
Length: 2,105 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleocapsid protein
UniProt: P03521
Pockets: 20 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Nucleocapsid protein	protein	421	44% helix, 6% strand	P03521

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	177	0.72	0.89	20	empty
2	167	0.67	0.87	21	empty
3	228	0.66	0.84	23	empty
4	709	0.65	0.74	79	empty
5	326	0.64	0.80	43	empty

Interfaces

7 interfaces between chains.

C–D · 2710 Å² buried · 25 hydrogen bonds · protein-protein
B–C · 2567 Å² buried · 21 hydrogen bonds · protein-protein
A–E · 2562 Å² buried · 26 hydrogen bonds · protein-protein
A–B · 2547 Å² buried · 22 hydrogen bonds · protein-protein
B–E · 328 Å² buried · 3 hydrogen bonds · protein-protein

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 P03521
Elsewhere: RCSB PDB 2QVJ · PDBe 2QVJ · UniProt P03521

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.