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X-ray structure of triatoma virus empty capsid

Analyse X-ray structure of triatoma virus empty capsid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5L7O
Type: protein
Length: 685 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein
UniProt: Q9QEY5
Pockets: 6 · best druggability 0.59

Structure

x-ray diffraction · 3 distinct chains · 11% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein	protein	230	11% helix, 31% strand	Q9QEY5
B	Capsid protein	protein	179	17% helix, 45% strand	Q9QEY5
C	Capsid protein	protein	276	6% helix, 36% strand	Q9QEY5

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	312	0.59	0.77	38	empty
2	187	0.54	0.79	26	empty
3	97	0.47	0.81	33	empty
4	105	0.40	0.76	18	empty
5	54	0.34	0.78	11	empty

Interfaces

3 interfaces between chains.

A–C · 3712 Å² buried · 55 hydrogen bonds · protein-protein
B–C · 1291 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 824 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

5L7O · X-ray structure of Triatoma virus empty capsid · 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 Q9QEY5
Elsewhere: RCSB PDB 5L7O · PDBe 5L7O · UniProt Q9QEY5

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