Structure of PDB 3ll8 Chain A

Receptor sequence
>3ll8A (length=357) Species: 9606 (Homo sapiens) [Search protein sequence]
TDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALR
IITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRY
LFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFK
QECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIR
KLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYP
AVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLD
VYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTE
MLVNVLN
3D structure
PDB3ll8 Balanced interactions of calcineurin with AKAP79 regulate Ca(2+)-calcineurin-NFAT signaling.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide A K100 M290 F299 P300 K318 N327 V328 M329 N330 I331 R332 Q333 K87 M277 F286 P287 K305 N314 V315 M316 N317 I318 R319 Q320
BS02 ZN A D118 N150 H199 H281 D105 N137 H186 H268
BS03 FE A D90 H92 D118 D77 H79 D105
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0033192 calmodulin-dependent protein phosphatase activity
Biological Process
GO:0097720 calcineurin-mediated signaling

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Molecular Function
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Biological Process
External links
PDB RCSB:3ll8, PDBe:3ll8, PDBj:3ll8
PDBsum3ll8
PubMed22343722
UniProtQ08209|PP2BA_HUMAN Protein phosphatase 3 catalytic subunit alpha (Gene Name=PPP3CA)

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