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Crystal structure analysis of the feline calicivirus capsid protein

Analyse Crystal structure analysis of the feline calicivirus capsid protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3M8L
Type: protein
Length: 1,598 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein
UniProt: A2T4Q0
Pockets: 20 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Capsid protein	protein	534	3% helix, 21% strand	A2T4Q0
B	Capsid protein	protein	530	8% helix, 21% strand	A2T4Q0

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	686	0.78	0.83	98	empty
2	460	0.76	0.85	70	empty
3	453	0.76	0.85	66	empty
4	115	0.74	0.93	28	empty
5	59	0.73	0.99	26	empty

Interfaces

3 interfaces between chains.

A–C · 1711 Å² buried · 14 hydrogen bonds · protein-protein
B–C · 1233 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 973 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

3M8L · Crystal Structure Analysis of the Feline Calicivirus Capsid Protein · 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 A2T4Q0
Elsewhere: RCSB PDB 3M8L · PDBe 3M8L · UniProt A2T4Q0

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