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Icosahedral reconstruction of the thermophilic bacteriophage P74-26 capsid

Analyse Icosahedral reconstruction of the thermophilic bacteriophage P74-26 capsid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6O3H
Type
protein
Length
3,878 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Major head protein; P74-26 head decoration protein
UniProt
A7XXR6, A7XXR5
Pockets
20 · best druggability 0.75

Structure

electron microscopy · 2 distinct chains · 16% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, GMajor head proteinprotein40919% helix, 27% strandA7XXR6
H, I, J, K, L, M, NP74-26 head decoration proteinprotein1458% helix, 28% strandA7XXR5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110590.750.78112empty
25850.700.7959empty
37600.700.7667empty
44910.690.7964empty
56880.690.7659empty

Interfaces

35 interfaces between chains.

  • D–E · 3376 Ų buried · 43 hydrogen bonds · protein-protein
  • A–F · 3353 Ų buried · 41 hydrogen bonds · protein-protein
  • B–C · 3350 Ų buried · 42 hydrogen bonds · protein-protein
  • A–B · 3326 Ų buried · 37 hydrogen bonds · protein-protein
  • C–D · 3293 Ų buried · 40 hydrogen bonds · protein-protein

Compared structures

  • 6O3H · Icosahedral reconstruction of the thermophilic bacteriophage P74-26 capsid · the same entry in another collection · chain A against A, TM-score 1.00

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