Structure of PDB 1vdn Chain A

Receptor sequence
>1vdnA (length=161) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
SQVYFDVEADGQPIGRVVFKLYNDIVPKTAENFRALCTGEKGFGYAGSPF
HRVIPDFMLQGGDFTAGNGTGGKSIYGGKFPDENFKKHHDRPGLLSMANA
GPNTNGSQFFITTVPCPWLDGKHVVFGEVVDGYDIVKKVESLGSPSGATK
ARIVVAKSGEL
3D structure
PDB1vdn Crystal Structure Of Yeast Cyclophilin A Complexed With ACE-Ala-Ala-Pro-Ala-7-Amino-4-Methylcoumarin
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R53 F58 Q61 N100 F111 L120 H124
Catalytic site (residue number reindexed from 1) R52 F57 Q60 N99 F110 L119 H123
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 R53 I55 F58 A99 N100 F111 L120 H124 R52 I54 F57 A98 N99 F110 L119 H123
Gene Ontology
Molecular Function
GO:0003729 mRNA binding
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0016018 cyclosporin A binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
GO:0006974 DNA damage response
GO:0009267 cellular response to starvation
GO:0015031 protein transport
GO:0030437 ascospore formation
GO:0045835 negative regulation of meiotic nuclear division
GO:0045836 positive regulation of meiotic nuclear division
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005758 mitochondrial intermembrane space
GO:0034967 Set3 complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1vdn, PDBe:1vdn, PDBj:1vdn
PDBsum1vdn
PubMed
UniProtP14832|CYPH_YEAST Peptidyl-prolyl cis-trans isomerase (Gene Name=CPR1)

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