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Fitting of the GP6 crystal structure into 3D cryo-EM reconstruction of bacteriophage T4 dome-shaped baseplate

Analyse Fitting of the GP6 crystal structure into 3D cryo-EM reconstruction of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3H3W
Type
protein
Length
3,900 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Baseplate structural protein GP6
UniProt
P19060
Pockets
20 · best druggability 0.77

Structure

electron microscopy · 2 distinct chains · 17% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, G, I, KBaseplate structural protein GP6protein32614% helix, 30% strandP19060
B, D, F, H, J, LBaseplate structural protein GP6protein32419% helix, 32% strandP19060

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19440.770.8096empty
211000.750.78109empty
35870.730.8070empty
45420.720.8165empty
57560.710.7777empty

Interfaces

18 interfaces between chains.

  • K–L · 1119 Ų buried · 14 hydrogen bonds · protein-protein
  • G–H · 1119 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 1115 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 1114 Ų buried · 14 hydrogen bonds · protein-protein
  • E–F · 1112 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 3H3W · Fitting of the gp6 crystal structure into 3D cryo-EM reconstruction of bacteriophage T4… · the same entry in another collection · chain A against A, TM-score 1.00

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