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Structure of the urea-treated empty bacteriophage T5 portal complex

Analyse Structure of the urea-treated empty bacteriophage T5 portal complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
9IMV
Type
protein
Length
6,480 residues
Chains
24
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
4.0
Source
Escherichia phage T5
Molecule
Portal protein pb7; Head completion protein
UniProt
Q6QGD5, Q6QGD9
Pockets
20 · best druggability 0.86

Structure

electron microscopy · resolution 4.0 · 2 distinct chains · 39% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LPortal protein pb7protein37043% helix, 13% strandQ6QGD5
M, N, O, P, Q, R, S, T, U, V, W, XHead completion proteinprotein17031% helix, 28% strandQ6QGD9

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19480.860.87120empty
29310.860.87112empty
311380.830.84137empty
410110.830.84115empty
511580.820.83136empty

Interfaces

77 interfaces between chains.

  • E–F · 5489 Ų buried · 68 hydrogen bonds · protein-protein
  • H–I · 5470 Ų buried · 69 hydrogen bonds · protein-protein
  • A–C · 5454 Ų buried · 75 hydrogen bonds · protein-protein
  • F–G · 5452 Ų buried · 69 hydrogen bonds · protein-protein
  • J–K · 5443 Ų buried · 68 hydrogen bonds · protein-protein

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