Research workbench

Human hepatitis B viral capsid (hbcag)

Analyse Human hepatitis B viral capsid (hbcag) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QGT
Type: protein
Length: 570 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (HBV capsid protein)
UniProt: Q67855
Pockets: 6 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 70% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, A	Protein (HBV capsid protein)	protein	142	72% helix, 0% strand	Q67855
D, B	Protein (HBV capsid protein)	protein	143	69% helix, 0% strand	Q67855

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	287	0.72	0.85	36	empty
2	240	0.72	0.87	29	empty
3	290	0.69	0.83	40	empty
4	75	0.34	0.75	14	empty
5	100	0.34	0.73	14	empty

Interfaces

3 interfaces between chains.

C–D · 2047 Å² buried · 24 hydrogen bonds · protein-protein
B–A · 2039 Å² buried · 20 hydrogen bonds · protein-protein
C–B · 574 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1QGT · Human hepatitis B viral capsid (hbcag) · the same entry in another collection · chain C against C, 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 Q67855
Elsewhere: RCSB PDB 1QGT · PDBe 1QGT · UniProt Q67855

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