Structure of PDB 1m63 Chain E Binding Site BS01

Receptor Information
>1m63 Chain E (length=359) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALR
IITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRY
LFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFK
QECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIR
KLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYP
AVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLD
VYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTE
MLVNVLNIC
Ligand information
>1m63 Chain H (length=11) Species: 29910 (Tolypocladium inflatum) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ALLVTPGLVLA
Receptor-Ligand Complex Structure
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PDB1m63 Crystal Structure of Calcineurin-Cyclophilin-Cyclosporin Shows Common But Distinct Recognition of Immunophilin-Drug Complexes
Resolution2.8 Å
Binding residue
(original residue number in PDB)		L312 Y341 P344 W352 F356
Binding residue
(residue number reindexed from 1)		L299 Y328 P331 W339 F343
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.
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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