Structure of PDB 2x7k Chain A Binding Site BS01
Receptor Information
>2x7k Chain A (length=164) Species:
9606
(Homo sapiens) [
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AIPPDSWQPPNVYLETSMGIIVLELYWKHAPKTCKNFAELARRGYYNGTK
FHRIIKDFMIQGGDPTGTGRGGASIYGKQFEDELHPDLKFTGAGILAMAN
AGPDTNGSQFFVTLAPTQWLDGKHTIFGRVCQGIGMVNRVGMVETNSQDR
PVDDVKIIKAYPSG
Ligand information
>2x7k Chain B (length=11) Species:
29910
(Tolypocladium inflatum) [
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ALLVTAGLVLA
Receptor-Ligand Complex Structure
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PDB
2x7k
The Crystal Structure of Ppil1 Bound to Cyclosporine a Suggests a Binding Mode for a Linear Epitope of the Skip Protein.
Resolution
1.15 Å
Binding residue
(original residue number in PDB)
R55 F60 Q63 G71 A101 N102 Q111 F113 W121 H126
Binding residue
(residue number reindexed from 1)
R53 F58 Q61 G69 A99 N100 Q109 F111 W119 H124
Enzymatic activity
Catalytic site (original residue number in PDB)
R55 F60 Q63 N102 F113 L122 H126
Catalytic site (residue number reindexed from 1)
R53 F58 Q61 N100 F111 L120 H124
Enzyme Commision number
5.2.1.8
: peptidylprolyl isomerase.
Gene Ontology
Molecular Function
GO:0003755
peptidyl-prolyl cis-trans isomerase activity
GO:0003824
catalytic activity
GO:0005515
protein binding
GO:0097718
disordered domain specific binding
Biological Process
GO:0000398
mRNA splicing, via spliceosome
GO:0000413
protein peptidyl-prolyl isomerization
GO:0006397
mRNA processing
GO:0006457
protein folding
GO:0008380
RNA splicing
GO:1990403
embryonic brain development
Cellular Component
GO:0005634
nucleus
GO:0005654
nucleoplasm
GO:0005681
spliceosomal complex
GO:0071007
U2-type catalytic step 2 spliceosome
GO:0071013
catalytic step 2 spliceosome
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External links
PDB
RCSB:2x7k
,
PDBe:2x7k
,
PDBj:2x7k
PDBsum
2x7k
PubMed
20368803
UniProt
Q9Y3C6
|PPIL1_HUMAN Peptidyl-prolyl cis-trans isomerase-like 1 (Gene Name=PPIL1)
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