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Human hepatitis B virus T=4 capsid strain adyw complexed with assembly effector HAP1

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

PDB: 2G34
Type: protein
Length: 582 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Core antigen
UniProt: P03147
Pockets: 10 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, B	Core antigen	protein	147	56% helix, 0% strand	P03147
D, A	Core antigen	protein	144	60% helix, 0% strand	P03147

Pockets

10 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	350	0.80	0.89	48	empty
2	523	0.79	0.85	59	empty
3	452	0.74	0.83	58	empty
4	257	0.69	0.84	39	empty
5	274	0.67	0.83	53	empty

Interfaces

3 interfaces between chains.

B–A · 1793 Å² buried · 14 hydrogen bonds · protein-protein
C–D · 1730 Å² buried · 14 hydrogen bonds · protein-protein
C–B · 657 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2G34 · Human hepatitis B virus T=4 capsid strain adyw complexed with assembly effector HAP1 · 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 2G34 · PDBe 2G34 · UniProt P03147

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