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Capsid structure of human sapovirus

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

PDB: 7DOD
Type: protein
Length: 1,573 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calicivirin
UniProt: A0A2Z6DUV0
Pockets: 15 · best druggability 0.80

Structure

electron microscopy · 2 distinct chains · 8% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, B	Calicivirin	protein	530	8% helix, 34% strand	A0A2Z6DUV0
A	Calicivirin	protein	513	8% helix, 32% strand	A0A2Z6DUV0

Pockets

15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1173	0.80	0.81	107	empty
2	1200	0.79	0.80	136	empty
3	1037	0.77	0.79	81	empty
4	519	0.73	0.82	55	empty
5	633	0.71	0.78	56	empty

Interfaces

3 interfaces between chains.

A–B · 1915 Å² buried · 20 hydrogen bonds · protein-protein
C–A · 1484 Å² buried · 13 hydrogen bonds · protein-protein
C–B · 1271 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

7DOD · Capsid structure of human sapovirus · 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 A0A2Z6DUV0
Elsewhere: RCSB PDB 7DOD · PDBe 7DOD · UniProt A0A2Z6DUV0

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