Structure of PDB 1m63 Chain E

Receptor sequence
>1m63E (length=359) Species: 9606 (Homo sapiens) [Search protein sequence]
TDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALR
IITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRY
LFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFK
QECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIR
KLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYP
AVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLD
VYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTE
MLVNVLNIC
3D structure
PDB1m63 Crystal Structure of Calcineurin-Cyclophilin-Cyclosporin Shows Common But Distinct Recognition of Immunophilin-Drug Complexes
ChainE
Resolution2.8 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) D77 H79 D105 D108 R109 N137 H138 H186 R241 H268
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 E L312 Y341 P344 W352 F356 L299 Y328 P331 W339 F343
BS02 ZN E D118 N150 H199 H281 D105 N137 H186 H268
BS03 FE E 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:1m63, PDBe:1m63, PDBj:1m63
PDBsum1m63
PubMed12218175
UniProtQ08209|PP2BA_HUMAN Protein phosphatase 3 catalytic subunit alpha (Gene Name=PPP3CA)

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