Structure of PDB 6nuc Chain A

Receptor sequence
>6nucA (length=361) Species: 9606 (Homo sapiens) [Search protein sequence]
KLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEES
VALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPA
NTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEY
FTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTL
DDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYF
YSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAP
NYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGE
KVTEMLVNVLN
3D structure
PDB6nuc Molecular basis for the binding and selective dephosphorylation of Na+/H+exchanger 1 by calcineurin.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D90 H92 D118 D121 R122 N150 H151 H199 R254 H281
Catalytic site (residue number reindexed from 1) D81 H83 D109 D112 R113 N141 H142 H190 R245 H272
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 F299 N327 V328 M329 N330 I331 Q333 W352 S353 F356 E359 K360 F290 N318 V319 M320 N321 I322 Q324 W343 S344 F347 E350 K351
BS02 FE A D90 H92 D118 D81 H83 D109
BS03 ZN A D118 N150 H199 H281 D109 N141 H190 H272
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
View graph for
Biological Process
External links
PDB RCSB:6nuc, PDBe:6nuc, PDBj:6nuc
PDBsum6nuc
PubMed31375679
UniProtQ08209|PP2BA_HUMAN Protein phosphatase 3 catalytic subunit alpha (Gene Name=PPP3CA)

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