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Cryo-EM structure of PCV2 vlps

Analyse Cryo-EM structure of PCV2 vlps in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5ZBO
Type
protein
Length
10,860 residues
Chains
60
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Capsid protein
UniProt
G0Y2B2
Pockets
20 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 2% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, 1, 2, 3, 4, 5, 6, 7, 8, 9, a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r, s, t, u, v, w, x, yCapsid proteinprotein1812% helix, 27% strandG0Y2B2

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11400.800.9725empty
26290.800.8555empty
36210.800.8556empty
41410.800.9727empty
56290.800.8559empty

Interfaces

150 interfaces between chains.

  • A–C · 1168 Ų buried · 13 hydrogen bonds · protein-protein
  • m–y · 1167 Ų buried · 13 hydrogen bonds · protein-protein
  • w–x · 1167 Ų buried · 13 hydrogen bonds · protein-protein
  • C–F · 1167 Ų buried · 12 hydrogen bonds · protein-protein
  • a–s · 1165 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 5ZBO · Cryo-EM structure of PCV2 VLPs · the same entry in another collection · chain h against h, TM-score 1.00

Analyse

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