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Cryoem structure of chimeric eastern equine encephalitis virus: genome-binding capsid N-terminal domain

Analyse Cryoem structure of chimeric eastern equine encephalitis virus: genome-binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MX7
Type: protein
Length: 699 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid
UniProt: P27284
Pockets: 3 · best druggability 0.58

Structure

electron microscopy · 3 distinct chains · 5% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	Capsid	protein	180	6% helix, 29% strand	P27284
F, I	Capsid	protein	171	7% helix, 38% strand	P27284
L	Capsid	protein	177	3% helix, 38% strand	P27284

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	324	0.58	0.77	45	empty
2	91	0.39	0.76	12	empty
3	59	0.30	0.75	15	empty

Interfaces

4 interfaces between chains.

C–I · 356 Å² buried · 11 hydrogen bonds · protein-protein
F–L · 182 Å² buried · 1 hydrogen bond · protein-protein
I–L · 166 Å² buried · 1 hydrogen bond · protein-protein
F–I · 31 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6MX7 · CryoEM structure of chimeric Eastern Equine Encephalitis Virus: Genome-Binding Capsid… · the same entry in another collection · chain C against C, 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 P27284
Elsewhere: RCSB PDB 6MX7 · PDBe 6MX7 · UniProt P27284

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