MolNFT v1 · #159897 · protein

Bile salts alter the mouse norovirus capsid conformation; possible implications for cell attachment and immune evasion.

6P4L · Capsid protein: “Bile salts alter the mouse norovirus capsid conformation; possible implications for cell attachment and…”. Electron microscopy, 4 pockets (best druggability 0.48). MolNFT v1 #159897 on GenesisL1: 3D structure…

PDB: 6P4L
Type: protein
Length: 601 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein
UniProt: Q2V8W4
Pockets: 4 · best druggability 0.48

Structure

electron microscopy · 3 distinct chains · 8% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein	protein	203	10% helix, 34% strand	Q2V8W4
B	Capsid protein	protein	205	6% helix, 30% strand	Q2V8W4
C	Capsid protein	protein	193	9% helix, 35% strand	Q2V8W4

Pockets

4 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	162	0.48	0.77	29	empty
2	64	0.41	0.81	18	empty
3	85	0.36	0.76	19	empty
4	68	0.30	0.74	16	empty

Interfaces

3 interfaces between chains.

A–C · 865 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 810 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 805 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6P4L · Bile salts alter the mouse norovirus capsid conformation; possible implications for cell… · 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 6P4L · PDBe 6P4L · UniProt Q2V8W4

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