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Cryo-EM structure of ATP-bound fully inactive ampk in complex with dorsomorphin (compound C) and Fab-nanobody

Analyse Cryo-EM structure of ATP-bound fully inactive ampk in complex with dorsomorphin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7JHG
Type
protein
Length
1,699 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
Q13131, O43741, P54619, C3SHQ8
Ligands
TAK, ATP, ADP, AMP, GLC

Structure

electron microscopy · 7 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein380—Q13131
B—protein93—O43741
G—protein300—P54619
M—protein367—C3SHQ8
L—protein211——
H—protein228——
N—protein120——

Ligands and binding sites

  • TAK · 6-[4-(2-piperidin-1-ylethoxy)phenyl]-3-pyridin-4-ylpyrazolo[1,5-a]pyrimidine · ligand · chains A
  • ATP · Adenosine-5'-triphosphate · ligand · chains G
  • ADP · Adenosine-5'-diphosphate · ligand · chains G
  • AMP · Adenosine monophosphate · ligand · chains G
  • GLC · alpha-D-glucopyranose · sugar · 2 copies · chains M

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

Compared structures

  • 7JHG · Cryo-EM structure of ATP-bound fully inactive AMPK in complex with Dorsomorphin (Compound… · the same entry in another collection · chain N against N, TM-score 1.00
  • P54619 · AlphaFold monomer V2.0 prediction for 5'-AMP-activated protein kinase subunit gamma-1… · a predicted model of the same protein · chain G against A, TM-score 0.96
  • O43741 · AlphaFold monomer V2.0 prediction for 5'-AMP-activated protein kinase subunit beta-2… · a predicted model of the same protein · chain B against A, TM-score 0.79
  • Q13131 · AlphaFold monomer V2.0 prediction for 5'-AMP-activated protein kinase catalytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.64

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