Structure of PDB 2oju Chain B Binding Site BS01

Receptor Information
>2oju Chain B (length=166) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SRVDGGMSVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCIFHR
NIKGFMVQTGDPTGTGRGGNSIWGKKFEDEYSEYLKHNVRGVVSMANNGP
NTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKTYRPL
NDVHIKDITIHANPFA
Ligand information
>2oju Chain D (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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PDB2oju Targeting Cyclophilin J, a Novel Peptidyl-Prolyl Isomerase, Can Induce Cellular G1/S Arrest and Repress the Growth of Hepatocellular Carcinoma
Resolution2.4 Å
Binding residue
(original residue number in PDB)		R50 F55 M56 Q58 G66 A96 N97 N98 Q106 F108 H116 Y121
Binding residue
(residue number reindexed from 1)		R50 F55 M56 Q58 G66 A96 N97 N98 Q106 F108 H116 Y121
Enzymatic activity
Catalytic site (original residue number in PDB) R50 F55 Q58 N97 F108 L117 Y121
Catalytic site (residue number reindexed from 1) R50 F55 Q58 N97 F108 L117 Y121
Enzyme Commision number 5.2.1.8: peptidylprolyl isomerase.
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005515 protein 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
Cellular Component
GO:0005654 nucleoplasm
GO:0005681 spliceosomal complex
GO:0071013 catalytic step 2 spliceosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2oju, PDBe:2oju, PDBj:2oju
PDBsum2oju
PubMed
UniProtQ9H2H8|PPIL3_HUMAN Peptidyl-prolyl cis-trans isomerase-like 3 (Gene Name=PPIL3)

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