Structure of PDB 2oju Chain A

Receptor sequence
>2ojuA (length=163) Species: 9606 (Homo sapiens) [Search protein sequence]
VDGGMSVTLHTDVGDIKIEVFCERTPKTCENFLALCASNYYNGCIFHRNI
KGFMVQTGDPTGTGRGGNSIWGKKFEDEYSEYLKHNVRGVVSMANNGPNT
NGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKTYRPLND
VHIKDITIHANPF
3D structure
PDB2oju Targeting Cyclophilin J, a Novel Peptidyl-Prolyl Isomerase, Can Induce Cellular G1/S Arrest and Repress the Growth of Hepatocellular Carcinoma
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R50 F55 Q58 N97 F108 L117 Y121
Catalytic site (residue number reindexed from 1) R48 F53 Q56 N95 F106 L115 Y119
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 R50 F55 M56 Q58 G66 A96 N97 N98 Q106 H116 Y121 R48 F53 M54 Q56 G64 A94 N95 N96 Q104 H114 Y119
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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