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Crystal structure of herpes simplex virus 1 PUL7:PUL51 complex

Analyse Crystal structure of herpes simplex virus 1 PUL7:PUL51 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6T5A
Type
protein
Length
1,488 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tegument protein UL51; Cytoplasmic envelopment protein 1
UniProt
D3YPL0, A0A110B4Q7
Ligands
CL
Pockets
20 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DTegument protein UL51protein9663% helix, 11% strandD3YPL0
E, F, G, HCytoplasmic envelopment protein 1protein27648% helix, 20% strandA0A110B4Q7

Ligands and binding sites

  • CL · Chloride ion · ion · 4 copies · chains E, F, G, H
  • GOL · Glycerol · additive · 4 copies · chains A, E, B, F, C, G, D, H

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18280.790.8278GOL, CL
211090.790.8084GOL, CL
310420.780.8082GOL, CL
45590.780.8576GOL, CL
58050.770.8041empty

Interfaces

26 interfaces between chains.

  • A–E · 2331 Ų buried · 32 hydrogen bonds · protein-protein
  • D–H · 2326 Ų buried · 32 hydrogen bonds · protein-protein
  • C–G · 2324 Ų buried · 32 hydrogen bonds · protein-protein
  • B–F · 2320 Ų buried · 32 hydrogen bonds · protein-protein
  • E–F · 588 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6T5A · Crystal structure of herpes simplex virus 1 pUL7:pUL51 complex · the same entry in another collection · chain A against A, TM-score 1.00

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