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Hepatitis B core protein.

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

PDB: 7OD4
Type: protein
Length: 591 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: External core antigen
UniProt: W6CP35
Pockets: 8 · best druggability 0.76

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, D	External core antigen	protein	151	64% helix, 1% strand	W6CP35
A	External core antigen	protein	143	67% helix, 0% strand	W6CP35
C	External core antigen	protein	146	64% helix, 1% strand	W6CP35

Pockets

8 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	225	0.76	0.90	38	empty
2	102	0.64	0.88	18	empty
3	137	0.62	0.85	23	empty
4	111	0.62	0.87	19	empty
5	145	0.56	0.82	27	empty

Interfaces

3 interfaces between chains.

B–A · 2057 Å² buried · 18 hydrogen bonds · protein-protein
C–D · 2034 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 1088 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

7OD4 · Hepatitis B core protein. · 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 W6CP35
Elsewhere: RCSB PDB 7OD4 · PDBe 7OD4 · UniProt W6CP35

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