Structure of PDB 2x7k Chain A

Receptor sequence
>2x7kA (length=164) Species: 9606 (Homo sapiens) [Search protein sequence]
AIPPDSWQPPNVYLETSMGIIVLELYWKHAPKTCKNFAELARRGYYNGTK
FHRIIKDFMIQGGDPTGTGRGGASIYGKQFEDELHPDLKFTGAGILAMAN
AGPDTNGSQFFVTLAPTQWLDGKHTIFGRVCQGIGMVNRVGMVETNSQDR
PVDDVKIIKAYPSG
3D structure
PDB2x7k The Crystal Structure of Ppil1 Bound to Cyclosporine a Suggests a Binding Mode for a Linear Epitope of the Skip Protein.
ChainA
Resolution1.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 R55 F60 Q63 G71 A101 N102 Q111 F113 W121 H126 R53 F58 Q61 G69 A99 N100 Q109 F111 W119 H124
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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Cellular Component
External links
PDB RCSB:2x7k, PDBe:2x7k, PDBj:2x7k
PDBsum2x7k
PubMed20368803
UniProtQ9Y3C6|PPIL1_HUMAN Peptidyl-prolyl cis-trans isomerase-like 1 (Gene Name=PPIL1)

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