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HBV D78S mutant capsid

Analyse HBV D78S mutant capsid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6W0K
Type: protein
Length: 546 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein
UniProt: P03147
Pockets: 7 · best druggability 0.70

Structure

electron microscopy · 4 distinct chains · 59% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Capsid protein	protein	137	56% helix, 0% strand	P03147
B	Capsid protein	protein	138	62% helix, 0% strand	P03147
C	Capsid protein	protein	136	63% helix, 0% strand	P03147
D	Capsid protein	protein	135	56% helix, 0% strand	P03147

Pockets

7 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	276	0.70	0.84	44	empty
2	70	0.45	0.82	17	empty
3	56	0.35	0.78	16	empty
4	74	0.35	0.75	14	empty
5	80	0.35	0.75	16	empty

Interfaces

3 interfaces between chains.

C–D · 2052 Å² buried · 15 hydrogen bonds · protein-protein
A–B · 2044 Å² buried · 11 hydrogen bonds · protein-protein
B–C · 651 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6W0K · HBV D78S mutant 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 P03147
Elsewhere: RCSB PDB 6W0K · PDBe 6W0K · UniProt P03147

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