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Fitting of GP9 structure into the bacteriophage T4 baseplate cryoem reconstruction

Analyse Fitting of GP9 structure into the bacteriophage T4 baseplate cryoem… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1PDP
Type
protein
Length
5,184 residues
Chains
18
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Baseplate structural protein GP9
UniProt
P10927
Pockets
7 · best druggability 0.32

Structure

electron microscopy · 1 distinct chain · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, RBaseplate structural protein GP9protein2880% helix, 0% strandP10927

Pockets

7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1780.320.7219empty
2540.280.7215empty
3500.280.7317empty
4500.270.7316empty
5530.270.7217empty

Interfaces

18 interfaces between chains.

  • J–K · 382 Ų buried · 0 hydrogen bonds · protein-protein
  • E–F · 381 Ų buried · 0 hydrogen bonds · protein-protein
  • P–Q · 381 Ų buried · 0 hydrogen bonds · protein-protein
  • G–H · 381 Ų buried · 0 hydrogen bonds · protein-protein
  • P–R · 381 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1PDP · Fitting of gp9 structure into the bacteriophage T4 baseplate cryoEM reconstruction · the same entry in another collection · chain A against A, TM-score 1.00

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