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Cryo-EM structure of murine norovirus (mnv-1)

Analyse Cryo-EM structure of murine norovirus (mnv-1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6S6L
Type: protein
Length: 1,510 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein
UniProt: Q2V8W4
Pockets: 15 · best druggability 0.77

Structure

electron microscopy · 3 distinct chains · 8% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein	protein	500	8% helix, 41% strand	Q2V8W4
B	Capsid protein	protein	508	9% helix, 37% strand	Q2V8W4
C	Capsid protein	protein	502	7% helix, 39% strand	Q2V8W4

Pockets

15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.77	0.99	21	empty
2	411	0.75	0.85	51	empty
3	334	0.69	0.83	49	empty
4	141	0.60	0.84	32	empty
5	116	0.59	0.85	27	empty

Interfaces

3 interfaces between chains.

A–B · 2893 Å² buried · 46 hydrogen bonds · protein-protein
B–C · 1548 Å² buried · 19 hydrogen bonds · protein-protein
A–C · 1251 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

6S6L · Cryo-EM structure of murine norovirus (MNV-1) · 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 Q2V8W4
Elsewhere: RCSB PDB 6S6L · PDBe 6S6L · UniProt Q2V8W4

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