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Mycobacteriophage Bxb1 Capsid - Composite map and model

Analyse Mycobacteriophage Bxb1 Capsid - Composite map and model in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 9D9X
Type: protein
Length: 4,263 residues
Chains: 11
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.0
Source: Mycobacterium phage Bxb1
Molecule: Major capsid protein
UniProt: Q9B0A7
Pockets: 20 · best druggability 0.76

Structure

electron microscopy · resolution 3.0 · 2 distinct chains · 22% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
Ha, Hb, Hc, Hd, He, Hf, Pb, Pc, Pd, Pe	Major capsid protein	protein	396	21% helix, 32% strand	Q9B0A7
Pa	Major capsid protein	protein	303	23% helix, 32% strand	Q9B0A7

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	446	0.76	0.85	63	empty
2	652	0.68	0.77	68	empty
3	586	0.68	0.77	65	empty
4	546	0.64	0.76	65	empty
5	675	0.64	0.74	53	empty

Interfaces

27 interfaces between chains.

Pd–Pe · 2713 Å² buried · 33 hydrogen bonds · protein-protein
He–Hf · 2697 Å² buried · 31 hydrogen bonds · protein-protein
Hc–Hd · 2672 Å² buried · 29 hydrogen bonds · protein-protein
Ha–Hb · 2621 Å² buried · 32 hydrogen bonds · protein-protein
Pb–Pc · 2607 Å² buried · 26 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 Q9B0A7
Elsewhere: RCSB PDB 9D9X · PDBe 9D9X · UniProt Q9B0A7

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