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Crystal structure of the molecular chaperone dnak from geobacillus kaustophilus HTA426 in post-ATP hydrolysis state

Analyse Crystal structure of the molecular chaperone dnak from geobacillus kaustophilus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2V7Y
Type
protein
Length
504 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chaperone protein dnak
UniProt
Q5KWZ7
Ligands
ADP, MG, PO4
Pockets
3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChaperone protein dnakprotein50434% helix, 33% strandQ5KWZ7

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • MG · Magnesium ion · metal · chains A
  • PO4 · Phosphate ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15390.740.8265ADP, PO4, MG
2800.430.8021empty
3980.420.7716empty

Compared structures

  • 2V7Y · Crystal structure of the molecular chaperone DnaK from Geobacillus kaustophilus HTA426 in… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5KWZ7 · AlphaFold monomer V2.0 prediction for chaperone protein dnak (Q5KWZ7) · a predicted model of the same protein · chain A against A, TM-score 0.65

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