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Crystal structure of the PRI1 subunit of human primase bound to ATP

Analyse Crystal structure of the PRI1 subunit of human primase bound to ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6R4S
Type
protein
Length
765 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DNA primase small subunit
EC
2.7.7.-
UniProt
P49642
Ligands
ATP, MN, ZN
Pockets
10 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADNA primase small subunit (EC 2.7.7.-)protein38247% helix, 12% strandP49642
EDNA primase small subunit (EC 2.7.7.-)protein38347% helix, 12% strandP49642

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, E
  • MN · Manganese (II) ion · metal · 4 copies · chains A, E
  • ZN · Zinc ion · metal · 2 copies · chains A, E

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

Pockets

10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16240.760.8263empty
24010.620.7743empty
3890.460.8116empty
41670.460.7621MN, ATP
51590.450.7628MN, ATP

Interfaces

1 interface between chains.

  • A–E · 996 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 6R4S · Crystal structure of the Pri1 subunit of human primase bound to ATP · the same entry in another collection · chain A against A, TM-score 1.00
  • P49642 · AlphaFold monomer V2.0 prediction for DNA primase small subunit (P49642) · a predicted model of the same protein · chain A against A, TM-score 0.97

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