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HBV pgrna T=4 ncp icosahedral symmetry

Analyse HBV pgrna T=4 ncp icosahedral symmetry in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ABL
Type: protein
Length: 578 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein
UniProt: Q765V7
Pockets: 7 · best druggability 0.74

Structure

electron microscopy · 3 distinct chains · 63% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Capsid protein	protein	144	62% helix, 0% strand	Q765V7
B	Capsid protein	protein	143	66% helix, 0% strand	Q765V7
D	Capsid protein	protein	147	61% helix, 0% strand	Q765V7

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	191	0.74	0.90	29	empty
2	79	0.63	0.90	20	empty
3	65	0.46	0.83	18	empty
4	73	0.32	0.74	14	empty
5	74	0.31	0.73	14	empty

Interfaces

3 interfaces between chains.

A–B · 2086 Å² buried · 16 hydrogen bonds · protein-protein
C–D · 2033 Å² buried · 13 hydrogen bonds · protein-protein
B–C · 611 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

7ABL · HBV pgRNA T=4 NCP icosahedral symmetry · 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 Q765V7
Elsewhere: RCSB PDB 7ABL · PDBe 7ABL · UniProt Q765V7

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