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MolNFT v1 · #29182 · protein

The glycogen-binding domain of the AMP-activated protein kinase BETA1 subunit

1Z0M · 5'-AMP-activated protein kinase, beta-1 subunit: “The glycogen-binding domain of the AMP-activated protein kinase BETA1 subunit”. X-ray diffraction, 1 ligand (GLC), 3 pockets (best druggability 0.47). MolNFT v1 #29182 on GenesisL1…

PDB
1Z0M
Type
protein
Length
248 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
5'-AMP-activated protein kinase, beta-1 subunit
UniProt
P80386
Ligands
GLC
Pockets
3 · best druggability 0.47

Structure

x-ray diffraction · 3 distinct chains · 4% helix, 58% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A5'-AMP-activated protein kinase, beta-1 subunitprotein873% helix, 56% strandP80386
B5'-AMP-activated protein kinase, beta-1 subunitprotein814% helix, 60% strandP80386
C5'-AMP-activated protein kinase, beta-1 subunitprotein804% helix, 59% strandP80386

Ligands and binding sites

  • GLC · alpha-D-glucopyranose · sugar · 21 copies · chains A, B, C

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11610.470.7622empty
2620.390.8014empty
3680.320.7516empty

Interfaces

3 interfaces between chains.

  • A–B · 584 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 340 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 15 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1Z0M · the glycogen-binding domain of the AMP-activated protein kinase beta1 subunit · the same entry in another collection · chain A against A, TM-score 1.00
  • P80386 · AlphaFold monomer V2.0 prediction for 5'-AMP-activated protein kinase subunit beta-1… · a predicted model of the same protein · chain C against A, TM-score 0.96

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