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Viral evolution results in multiple, surface-allocated enzymatic activities in a fungal double-stranded RNA virus

Analyse Viral evolution results in multiple, surface-allocated enzymatic activities in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ND1
Type: protein
Length: 1,977 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein
UniProt: M1VMJ0, M1VHN2
Pockets: 20 · best druggability 0.83

Structure

electron microscopy · 2 distinct chains · 29% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein	protein	972	28% helix, 14% strand	M1VMJ0
B	Capsid protein	protein	1005	30% helix, 11% strand	M1VHN2

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1151	0.83	0.84	137	empty
2	996	0.79	0.81	75	empty
3	92	0.75	0.97	27	empty
4	559	0.66	0.77	46	empty
5	279	0.65	0.82	36	empty

Interfaces

1 interface between chains.

A–B · 8090 Å² buried · 78 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 isopeptide (isopeptide).

Compared structures

5ND1 · Viral evolution results in multiple, surface-allocated enzymatic activities in a fungal… · 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 M1VMJ0
Every structure of UniProt M1VHN2
Elsewhere: RCSB PDB 5ND1 · PDBe 5ND1 · UniProt M1VMJ0 · UniProt M1VHN2

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