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Icosahedral symmetry reconstruction of brome mosaic virus (RNA 3+4)

Analyse Icosahedral symmetry reconstruction of brome mosaic virus (RNA 3+4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VOC
Type: protein
Length: 476 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein
UniProt: P03602
Pockets: 7 · best druggability 0.57

Structure

electron microscopy · 3 distinct chains · 9% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Capsid protein	protein	163	7% helix, 36% strand	P03602
C	Capsid protein	protein	164	10% helix, 36% strand	P03602
A	Capsid protein	protein	149	9% helix, 39% strand	P03602

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	326	0.57	0.76	33	empty
2	282	0.55	0.76	40	empty
3	298	0.53	0.75	27	empty
4	189	0.52	0.78	25	empty
5	57	0.39	0.81	11	empty

Interfaces

3 interfaces between chains.

C–A · 582 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 532 Å² buried · 5 hydrogen bonds · protein-protein
B–A · 498 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6VOC · icosahedral symmetry reconstruction of brome mosaic virus (RNA 3+4) · the same entry in another collection · chain B against B, 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 P03602
Elsewhere: RCSB PDB 6VOC · PDBe 6VOC · UniProt P03602

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