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The crystal structure of the bifunctional primase-helicase of bacteriophage T7

Analyse The crystal structure of the bifunctional primase-helicase of bacteriophage T7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1Q57
Type
protein
Length
3,381 residues
Chains
7
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DNA PRIMASE/HELICASE
EC
2.7.7.-
UniProt
P03692
Pockets
20 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, GDNA PRIMASE/HELICASE (EC 2.7.7.-)protein48333% helix, 23% strandP03692

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16980.810.8572empty
211680.810.82112empty
310560.810.8294empty
43810.800.9052empty
510780.800.8292empty

Interfaces

7 interfaces between chains.

  • F–G · 2024 Ų buried · 23 hydrogen bonds · protein-protein
  • B–G · 1972 Ų buried · 30 hydrogen bonds · protein-protein
  • C–D · 1851 Ų buried · 31 hydrogen bonds · protein-protein
  • D–E · 1754 Ų buried · 28 hydrogen bonds · protein-protein
  • A–B · 1673 Ų buried · 21 hydrogen bonds · protein-protein

Compared structures

  • 1Q57 · The Crystal Structure of the Bifunctional Primase-Helicase of Bacteriophage T7 · the same entry in another collection · chain A against A, TM-score 1.00

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