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The crystal structure of the ARGONAUTE2 paz domain (as a mbp fusion)

Analyse The crystal structure of the ARGONAUTE2 paz domain (as a mbp fusion) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1R6Z
Type
protein
Length
1,494 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chimera of maltose-binding periplasmic protein and argonaute 2
UniProt
P02928
Ligands
GLC, NI
Pockets
18 · best druggability 0.71

Structure

x-ray diffraction · 3 distinct chains · 41% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
PChimera of maltose-binding periplasmic protein and argonaute 2protein49842% helix, 22% strandP02928
AChimera of maltose-binding periplasmic protein and argonaute 2protein49741% helix, 22% strandP02928
ZChimera of maltose-binding periplasmic protein and argonaute 2protein49941% helix, 22% strandP02928

Ligands and binding sites

  • GLC · alpha-D-glucopyranose · sugar · 6 copies · chains P, A, Z
  • NI · Nickel (II) ion · metal · 9 copies · chains P, A, Z

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12750.710.8530GLC
22910.700.8431GLC
32620.690.8426GLC
44650.600.7549empty
55090.600.7453empty

Interfaces

3 interfaces between chains.

  • P–A · 215 Ų buried · 2 hydrogen bonds · protein-protein
  • P–Z · 198 Ų buried · 1 hydrogen bond · protein-protein
  • A–Z · 173 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1R6Z · The Crystal Structure of the Argonaute2 PAZ domain (as a MBP fusion) · the same entry in another collection · chain P against P, TM-score 1.00

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