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Crystal structure of herpes simplex UL42 bound to the C-terminus of HSV pol

Analyse Crystal structure of herpes simplex UL42 bound to the C-terminus of HSV pol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1DML
Type
protein
Length
1,233 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DNA polymerase processivity factor; DNA polymerase
EC
2.7.7.7
UniProt
P10226, P07917
Pockets
12 · best druggability 0.85

Structure

x-ray diffraction · 4 distinct chains · 17% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADNA polymerase processivity factorprotein26713% helix, 42% strandP10226
B, D, F, HDNA polymerase (EC 2.7.7.7)protein3664% helix, 11% strandP07917
CDNA polymerase processivity factorprotein27215% helix, 42% strandP10226
E, GDNA polymerase processivity factorprotein27516% helix, 42% strandP10226

Pockets

12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18460.850.88106empty
21940.660.8525empty
31860.660.8627empty
42740.620.8032empty
52180.530.7726empty

Interfaces

10 interfaces between chains.

  • A–B · 1413 Ų buried · 22 hydrogen bonds · protein-protein
  • G–H · 1409 Ų buried · 15 hydrogen bonds · protein-protein
  • E–F · 1405 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 1401 Ų buried · 23 hydrogen bonds · protein-protein
  • A–E · 928 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 1DML · Crystal structure of herpes simplex UL42 bound to the C-terminus of HSV pol · the same entry in another collection · chain A against A, TM-score 1.00

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