MolNFT v1 · #151642 · protein

Wt hepatitis B core protein capsid

6HTX · Capsid protein: “Wt hepatitis B core protein capsid”. Electron microscopy, 7 pockets (best druggability 0.80). MolNFT v1 #151642 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6HTX
Type: protein
Length: 591 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein
UniProt: P03146
Pockets: 7 · best druggability 0.80

Structure

electron microscopy · 3 distinct chains · 68% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, D	Capsid protein	protein	151	65% helix, 1% strand	P03146
A	Capsid protein	protein	143	67% helix, 0% strand	P03146
C	Capsid protein	protein	146	71% helix, 1% strand	P03146

Pockets

7 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	145	0.80	0.96	28	empty
2	94	0.61	0.87	16	empty
3	105	0.60	0.86	17	empty
4	111	0.56	0.84	16	empty
5	78	0.53	0.85	18	empty

Interfaces

3 interfaces between chains.

B–A · 2086 Å² buried · 14 hydrogen bonds · protein-protein
C–D · 2077 Å² buried · 18 hydrogen bonds · protein-protein
B–C · 1150 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6HTX · WT Hepatitis B core protein capsid · 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 6HTX · PDBe 6HTX · UniProt P03146

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