Structure of PDB 1m63 Chain A Binding Site BS01
Receptor Information
>1m63 Chain A (length=372) Species:
9606
(Homo sapiens) [
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MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHL
MKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMK
LFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGN
HECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHG
GLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTH
NTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFP
SLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVF
TWSLPFVGEKVTEMLVNVLNIC
Ligand information
>1m63 Chain D (length=11) Species:
29910
(Tolypocladium inflatum) [
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ALLVTPGLVLA
Receptor-Ligand Complex Structure
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PDB
1m63
Crystal Structure of Calcineurin-Cyclophilin-Cyclosporin Shows Common But Distinct Recognition of Immunophilin-Drug Complexes
Resolution
2.8 Å
Binding residue
(original residue number in PDB)
Y341 P344 W352 F356
Binding residue
(residue number reindexed from 1)
Y341 P344 W352 F356
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)
D90 H92 D118 D121 R122 N150 H151 H199 R254 H281
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
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:1m63
,
PDBe:1m63
,
PDBj:1m63
PDBsum
1m63
PubMed
12218175
UniProt
Q08209
|PP2BA_HUMAN Protein phosphatase 3 catalytic subunit alpha (Gene Name=PPP3CA)
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