Structure of PDB 1e3b Chain A

Receptor sequence
>1e3bA (length=172) Species: 6239 (Caenorhabditis elegans) [Search protein sequence]
MSRSKVFFDITIGGKASGRIVMELYDDVVPKTAGNFRALCTGENGIGKSG
KPLHFKGSKFHRIIPNFMIQGGDFTRGNGTGGESIYGEKFPDENFKEKHT
GPGVLSMANAGPNTNGSQFFLCTVKTEWLDGKHVVFGRVVEGLDVVKAVE
SNGSQSGKPVKDCMIADCGQLK
3D structure
PDB1e3b First Crystal Structure of a Medicinally Relevant Gold Protein Complex:Unexpected Binding of [Au(Pet (3))](+) to Histidine
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R62 F67 Q70 N109 F120 L129 H133
Catalytic site (residue number reindexed from 1) R62 F67 Q70 N109 F120 L129 H133
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 3EP A W128 K132 W128 K132
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005515 protein binding
GO:0016018 cyclosporin A binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion

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Cellular Component
External links
PDB RCSB:1e3b, PDBe:1e3b, PDBj:1e3b
PDBsum1e3b
PubMed11028014
UniProtP52011|CYP3_CAEEL Peptidyl-prolyl cis-trans isomerase 3 (Gene Name=cyn-3)

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