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

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

PDB
6R5D
Type
protein
Length
769 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
DTP, MN, ZN
Pockets
12 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADNA primase small subunit (EC 2.7.7.-)protein38448% helix, 12% strandP49642
EDNA primase small subunit (EC 2.7.7.-)protein38550% helix, 12% strandP49642

Ligands and binding sites

  • DTP · 2'-deoxyadenosine 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
  • EDO · 1,2-ethanediol · additive · 11 copies · chains A, E

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111460.760.7896EDO
21120.480.8015empty
31850.470.7622MN, DTP
41740.450.7528MN, DTP
5770.440.8114EDO

Interfaces

1 interface between chains.

  • A–E · 1005 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 6R5D · Crystal structure of the Pri1 subunit of human primase bound to dATP · 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 E against A, TM-score 0.97

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