Structure of PDB 3ll8 Chain A Binding Site BS02
Receptor Information
>3ll8 Chain A (length=357) Species:
9606
(Homo sapiens) [
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TDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALR
IITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRY
LFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFK
QECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIR
KLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYP
AVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLD
VYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTE
MLVNVLN
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
3ll8 Chain A Residue 505 [
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Receptor-Ligand Complex Structure
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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)
D118 N150 H199 H281
Binding residue
(residue number reindexed from 1)
D105 N137 H186 H268
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
View graph for
Molecular Function
View graph for
Biological Process
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)
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