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Cryoem structure of rotavirus NSP2

Analyse Cryoem structure of rotavirus NSP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7PKO
Type: protein
Length: 2,504 residues
Chains: 8
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-structural protein 2
EC: 3.6.4.-
UniProt: A2T3N6
Pockets: 20 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 37% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, U	Non-structural protein 2 (EC 3.6.4.-)	protein	313	37% helix, 15% strand	A2T3N6

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	355	0.84	0.93	51	empty
2	466	0.84	0.91	59	empty
3	286	0.84	0.94	51	empty
4	343	0.83	0.93	51	empty
5	1019	0.79	0.81	75	empty

Interfaces

16 interfaces between chains.

C–F · 1500 Å² buried · 7 hydrogen bonds · protein-protein
A–D · 1464 Å² buried · 6 hydrogen bonds · protein-protein
E–U · 1422 Å² buried · 5 hydrogen bonds · protein-protein
B–G · 1383 Å² buried · 6 hydrogen bonds · protein-protein
F–G · 748 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

7PKO · CryoEM structure of Rotavirus NSP2 · 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 A2T3N6
Elsewhere: RCSB PDB 7PKO · PDBe 7PKO · UniProt A2T3N6

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