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Hepatitis B core protein -low secretion phenotype L60V

Analyse Hepatitis B core protein -low secretion phenotype L60V in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7OCO
Type: protein
Length: 591 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein
UniProt: P03146
Pockets: 6 · best druggability 0.78

Structure

electron microscopy · 3 distinct chains · 65% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, D	Capsid protein	protein	151	61% helix, 1% strand	P03146
A	Capsid protein	protein	143	66% helix, 0% strand	P03146
C	Capsid protein	protein	146	68% helix, 1% strand	P03146

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	139	0.78	0.95	29	empty
2	60	0.46	0.83	21	empty
3	56	0.37	0.79	14	empty
4	74	0.32	0.74	14	empty
5	63	0.30	0.74	15	empty

Interfaces

3 interfaces between chains.

B–A · 2041 Å² buried · 11 hydrogen bonds · protein-protein
C–D · 2021 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 1075 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

7OCO · Hepatitis B core protein -low secretion phenotype L60V · the same entry in another collection · chain B against B, 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 P03146
Elsewhere: RCSB PDB 7OCO · PDBe 7OCO · UniProt P03146

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