› 4y0g

X-ray diffraction
1.6Å resolution

beta2 carbohydrate binding module (CBM) of AMP-activated protein kinase (AMPK)

Released:
DOI: 10.2210/pdb4y0g/pdb
Model geometry
Fit model/data
PDB entry 4y0g coloured by chain, front view.
PDB entry 4y0g coloured by chain, side view.
PDB entry 4y0g coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Determinants of oligosaccharide specificity of the carbohydrate-binding modules of AMP-activated protein kinase.
Mobbs JI, Koay A, Di Paolo A, Bieri M, Petrie EJ, Gorman MA, Doughty L, Parker MW, Stapleton DI, Griffin MD, Gooley PR
Biochem J 468 245-57 (2015)
PMID: 25774984

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193068 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5'-AMP-activated protein kinase subunit beta-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 90 amino acids
Theoretical weight: 10.02 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9QZH4 (Residues: 74-155; Coverage: 30%)
Gene name: Prkab2
Sequence domains: Glycogen recognition site of AMP-activated protein kinase
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:
Ligand GOL 9 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: C2
Unit cell:
a: 112.973Å b: 27.627Å c: 78.882Å
α: 90° β: 133.88° γ: 90°
R-values:
R R work R free
0.152 0.15 0.182
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

AMP-activated protein kinase: a cellular energy sensor that comes in 12 flavours.
Ross et al. (2016)
5 more