Structure of PDB 2p6b Chain C

Receptor sequence
>2p6bC (length=357) Species: 9606 (Homo sapiens) [Search protein sequence]
TDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALR
IITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRY
LFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFK
QECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIR
KLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYP
AVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLD
VYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTE
MLVNVLN
3D structure
PDB2p6b Structure of calcineurin in complex with PVIVIT peptide: Portrait of a low-affinity signalling interaction
ChainC
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G106 P108 W134 K137 I138 C166 K167 H199
Catalytic site (residue number reindexed from 1) G93 P95 W121 K124 I125 C153 K154 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 C F299 K318 N327 V328 M329 N330 I331 F286 K305 N314 V315 M316 N317 I318
BS02 ZN C D118 N150 H199 H281 D105 N137 H186 H268
BS03 FE C 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:2p6b, PDBe:2p6b, PDBj:2p6b
PDBsum2p6b
PubMed17498738
UniProtQ08209|PP2BA_HUMAN Protein phosphatase 3 catalytic subunit alpha (Gene Name=PPP3CA)

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