Structure of PDB 3ll8 Chain A Binding Site BS03

Receptor Information

>3ll8 Chain A (length=357) Species: 9606 (Homo sapiens)

TDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALR
IITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRY
LFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFK
QECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIR
KLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYP
AVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLD
VYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTE
MLVNVLN

Ligand information

• Ligand ID: FE
• InChI: InChI=1S/Fe/q+3
• InChIKey: VTLYFUHAOXGGBS-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  CACTVS 3.341
  OpenEye OEToolkits 1.5.0: [Fe+3]
• Formula: Fe
• Name: FE (III) ION
• DrugBank: DB13949
• PDB chain: 3ll8 Chain A Residue 506

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3ll8 Balanced interactions of calcineurin with AKAP79 regulate Ca(2+)-calcineurin-NFAT signaling.
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): D90 H92 D118
• Binding residue (residue number reindexed from 1): D77 H79 D105
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H199
• Catalytic site (residue number reindexed from 1): H186
• Enzyme Commision number: 3.1.3.16: protein-serine/threonine phosphatase.

Gene Ontology

Molecular Function

• GO:0016787 hydrolase activity
• GO:0033192 calmodulin-dependent protein phosphatase activity

Biological Process

• GO:0097720 calcineurin-mediated signaling

External links

• PDB: RCSB:3ll8, PDBe:3ll8, PDBj:3ll8
• PDBsum: 3ll8
• PubMed: 22343722
• UniProt: Q08209|PP2BA_HUMAN Protein phosphatase 3 catalytic subunit alpha (Gene Name=PPP3CA)