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Topological model of P2 virion baseplate in activated conformation

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

PDB
6ZIH
Type
protein
Length
9,426 residues
Chains
33
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Distal tail protein; Baseplate protein GP16; Receptor binding protein
UniProt
D3WAD3, D3KFX4, Q71AW2
Pockets
20 · best druggability 0.58

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
2, 3, 7, 6, 5, 4, S, T, U, V, W, XDistal tail proteinprotein2980% helix, 0% strandD3WAD3
1, Y, ZBaseplate protein GP16protein3720% helix, 0% strandD3KFX4
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, RReceptor binding proteinprotein2630% helix, 0% strandQ71AW2

Pockets

20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13710.580.7471empty
23260.560.7361empty
32280.530.7550empty
42380.520.7445empty
52130.490.7353empty

Interfaces

74 interfaces between chains.

  • E–F · 573 Ų buried · 0 hydrogen bonds · protein-protein
  • J–K · 573 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 572 Ų buried · 0 hydrogen bonds · protein-protein
  • N–O · 571 Ų buried · 0 hydrogen bonds · protein-protein
  • K–L · 571 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6ZIH · Topological model of p2 virion baseplate in activated conformation · the same entry in another collection · chain 3 against 3, TM-score 1.00

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