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Threonine 204 of the chaperone protein HSC70 influences the structure of the active site but is not essential for ATP hydrolysis

Analyse Threonine 204 of the chaperone protein HSC70 influences the structure of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ATR
Type
protein
Length
383 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heat-shock cognate 70 kd protein
EC
3.6.1.3
UniProt
P19120
Ligands
ADP, MG, PO4
Pockets
1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHeat-shock cognate 70 kd protein (EC 3.6.1.3)protein38339% helix, 28% strandP19120

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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18360.780.8283MG, PO4, ADP

Compared structures

  • 1ATR · Threonine 204 of the chaperone protein HSC70 influences the structure of the active site… · the same entry in another collection · chain A against A, TM-score 1.00
  • P19120 · AlphaFold monomer V2.0 prediction for heat shock cognate 71 kda protein (P19120) · a predicted model of the same protein · chain A against A, TM-score 0.88

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