Research workbench

African swine fever virus major capsid protein P72

Analyse African swine fever virus major capsid protein P72 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6L2T
Type: protein
Length: 1,889 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: B646L,MAJOR capsid protein
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 2 distinct chains · 9% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	B646L,MAJOR capsid protein	protein	628	10% helix, 17% strand	—
C	B646L,MAJOR capsid protein	protein	633	9% helix, 16% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1059	0.87	0.87	111	empty
2	1083	0.86	0.87	133	empty
3	1175	0.86	0.87	137	empty
4	961	0.85	0.86	83	empty
5	1154	0.83	0.83	119	empty

Interfaces

3 interfaces between chains.

B–C · 5822 Å² buried · 25 hydrogen bonds · protein-protein
A–C · 5572 Å² buried · 22 hydrogen bonds · protein-protein
A–B · 5549 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

6L2T · African swine fever virus major capsid protein p72 · 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
Elsewhere: RCSB PDB 6L2T · PDBe 6L2T

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