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Crystal structure of the archaeal holliday junction resolvase hjc

Analyse Crystal structure of the archaeal holliday junction resolvase hjc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GEF
Type
protein
Length
459 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Holliday junction resolvase
UniProt
Q9V301
Ligands
SO4
Pockets
2 · best druggability 0.81

Structure

x-ray diffraction · 4 distinct chains · 33% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHolliday junction resolvaseprotein12036% helix, 33% strandQ9V301
BHolliday junction resolvaseprotein11630% helix, 34% strandQ9V301
DHolliday junction resolvaseprotein10935% helix, 30% strandQ9V301
EHolliday junction resolvaseprotein11430% helix, 34% strandQ9V301

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains A, B, D, E

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111660.810.82110SO4
21200.460.7926empty

Interfaces

4 interfaces between chains.

  • B–D · 870 Ų buried · 19 hydrogen bonds · protein-protein
  • A–E · 868 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 663 Ų buried · 22 hydrogen bonds · protein-protein
  • D–E · 648 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

  • 1GEF · Crystal structure of the archaeal holliday junction resolvase HJC · the same entry in another collection · chain B against B, TM-score 1.00

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