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Human hepatitis B virus T=4 capsid, strain adyw

Analyse Human hepatitis B virus T=4 capsid, strain adyw in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2G33
Type: protein
Length: 588 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Core antigen
UniProt: P03147
Pockets: 13 · best druggability 0.80

Structure

x-ray diffraction · 3 distinct chains · 55% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, B	Core antigen	protein	147	53% helix, 0% strand	P03147
D	Core antigen	protein	146	52% helix, 0% strand	P03147
A	Core antigen	protein	148	61% helix, 0% strand	P03147

Pockets

13 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	396	0.80	0.88	44	empty
2	295	0.78	0.89	42	empty
3	360	0.69	0.82	39	empty
4	139	0.64	0.86	28	empty
5	138	0.60	0.84	25	empty

Interfaces

3 interfaces between chains.

C–D · 1823 Å² buried · 10 hydrogen bonds · protein-protein
B–A · 1778 Å² buried · 12 hydrogen bonds · protein-protein
C–B · 650 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2G33 · Human Hepatitis B Virus T=4 capsid, strain adyw · 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 P03147
Elsewhere: RCSB PDB 2G33 · PDBe 2G33 · UniProt P03147

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