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Topological model of P2 virion baseplate in resting conformation

Analyse Topological model of P2 virion baseplate in resting conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ZJJ
Type
protein
Length
9,435 residues
Chains
33
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Distal tail protein; Receptor binding protein; Baseplate protein GP16
UniProt
D3WAD3, Q71AW2, D3KFX4
Pockets
20 · best druggability 0.61

Structure

electron microscopy · 3 distinct chains · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
T, S, U, V, W, X, 2, 3, 4, 5, 6, 7Distal tail proteinprotein2980% helix, 0% strandD3WAD3
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, RReceptor binding proteinprotein2630% helix, 0% strandQ71AW2
Y, Z, 1Baseplate protein GP16protein3750% helix, 0% strandD3KFX4

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14600.610.7379empty
23950.590.7384empty
33860.590.7375empty
43350.570.7468empty
53240.560.7367empty

Interfaces

57 interfaces between chains.

  • M–N · 572 Ų buried · 0 hydrogen bonds · protein-protein
  • D–E · 570 Ų buried · 0 hydrogen bonds · protein-protein
  • A–B · 569 Ų buried · 0 hydrogen bonds · protein-protein
  • P–Q · 569 Ų buried · 0 hydrogen bonds · protein-protein
  • J–K · 569 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6ZJJ · Topological model of p2 virion baseplate in resting conformation · the same entry in another collection · chain A against A, TM-score 1.00

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