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MolNFT v1 · #171844 · protein

Topological model of the P2 virion baseplate in activated conformation (closed tal trimer)

6ZIG · Receptor binding protein: “Topological model of the P2 virion baseplate in activated conformation (closed tal trimer)”. Electron microscopy, 20 pockets (best druggability 0.55). MolNFT v1 #171844 on GenesisL1: 3D structure, binding…

PDB
6ZIG
Type
protein
Length
9,435 residues
Chains
33
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Receptor binding protein; Distal tail protein; Baseplate protein GP16
UniProt
Q71AW2, D3WAD3, D3KFX4
Pockets
20 · best druggability 0.55

Structure

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

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13210.550.7370empty
22550.530.7453empty
32340.520.7450empty
42360.510.7352empty
52020.490.7450empty

Interfaces

65 interfaces between chains.

  • B–C · 575 Ų buried · 0 hydrogen bonds · protein-protein
  • E–F · 575 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 573 Ų buried · 0 hydrogen bonds · protein-protein
  • K–L · 571 Ų buried · 0 hydrogen bonds · protein-protein
  • N–O · 570 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6ZIG · Topological model of the p2 virion baseplate in activated conformation (closed Tal trimer) · the same entry in another collection · chain B against B, TM-score 1.00

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