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Crystal structure of the pria protein complexed with oligonucleotides

Analyse Crystal structure of the pria protein complexed with oligonucleotides in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2DWM
Type
protein + DNA
Length
421 residues
Chains
7
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
5'-D(*AP*T)-3'; Primosomal protein N
EC
3.6.1.-
UniProt
P17888
Pockets
8 · best druggability 0.73

Structure

x-ray diffraction · 5 distinct chains · 24% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
E, G5'-D(*AP*T)-3'dna1——
F5'-D(*AP*T)-3'dna2——
A, CPrimosomal protein N (EC 3.6.1.-)protein10525% helix, 22% strandP17888
BPrimosomal protein N (EC 3.6.1.-)protein10425% helix, 21% strandP17888
DPrimosomal protein N (EC 3.6.1.-)protein10323% helix, 26% strandP17888

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16230.730.8053empty
21980.520.7721empty
3960.460.8019empty
4970.430.7920empty
51140.430.7719empty

Interfaces

11 interfaces between chains.

  • C–D · 2137 Ų buried · 39 hydrogen bonds · protein-protein
  • A–B · 2088 Ų buried · 33 hydrogen bonds · protein-protein
  • A–C · 800 Ų buried · 10 hydrogen bonds · protein-protein
  • F–C · 318 Ų buried · 9 hydrogen bonds · protein-nucleic
  • E–A · 247 Ų buried · 6 hydrogen bonds · protein-nucleic

Compared structures

  • 2DWM · Crystal structure of the PriA protein complexed with oligonucleotides · the same entry in another collection · chain A against A, TM-score 1.00
  • P17888 · AlphaFold monomer V2.0 prediction for primosomal protein N' (P17888) · a predicted model of the same protein · chain D against A, TM-score 0.84

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