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Mature mlv capsid pentamer structure in intact virus particles

Analyse Mature mlv capsid pentamer structure in intact virus particles in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HWY
Type: protein
Length: 944 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative gag polyprotein
UniProt: A0A240FAQ8
Pockets: 5 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 60% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Putative gag polyprotein	protein	236	60% helix, 3% strand	A0A240FAQ8

Pockets

5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1014	0.80	0.82	110	empty
2	922	0.79	0.81	117	empty
3	1189	0.78	0.80	113	empty
4	688	0.71	0.78	71	empty
5	649	0.67	0.76	66	empty

Interfaces

4 interfaces between chains.

C–D · 378 Å² buried · 2 hydrogen bonds · protein-protein
A–B · 308 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 226 Å² buried · 0 hydrogen bonds · protein-protein
A–C · 58 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6HWY · Mature MLV capsid pentamer structure in intact virus particles · 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 A0A240FAQ8
Elsewhere: RCSB PDB 6HWY · PDBe 6HWY · UniProt A0A240FAQ8

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