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Bacteriophage HRP29 Procapsid Icosohedral Reconstruction

Analyse Bacteriophage HRP29 Procapsid Icosohedral Reconstruction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8EM6
Type: protein
Length: 2,128 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.5
Source: Shigella phage Buco
Molecule: Gp37
UniProt: A0A482JKU4
Pockets: 20 · best druggability 0.81

Structure

electron microscopy · resolution 3.5 · 1 distinct chain · 28% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G	Gp37	protein	304	28% helix, 24% strand	A0A482JKU4

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1040	0.81	0.82	118	empty
2	873	0.79	0.82	103	empty
3	1001	0.78	0.80	106	empty
4	1005	0.77	0.79	97	empty
5	1166	0.77	0.79	110	empty

Interfaces

9 interfaces between chains.

E–F · 1212 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 1106 Å² buried · 5 hydrogen bonds · protein-protein
D–E · 1105 Å² buried · 2 hydrogen bonds · protein-protein
A–F · 1052 Å² buried · 5 hydrogen bonds · protein-protein
B–C · 1023 Å² buried · 6 hydrogen bonds · protein-protein

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 A0A482JKU4
Elsewhere: RCSB PDB 8EM6 · PDBe 8EM6 · UniProt A0A482JKU4

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