Structure of PDB 2esl Chain A

Receptor sequence
>2eslA (length=181) Species: 9606 (Homo sapiens) [Search protein sequence]
RGPSVTAKVFFDVRIGDKDVGRIVIGLFGKVVPKTVENFVALATGEKGYG
YKGSKFHRVIKDFMIQGGDITTGDGTGGVSIYGETFPDENFKLKHYGIGW
VSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQAT
DGHDRPLTNCSIINSGKIDVKTPFVVEIADW
3D structure
PDB2esl Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R89 F94 Q97 N136 F147 L156 H160
Catalytic site (residue number reindexed from 1) R58 F63 Q66 N105 F116 L125 H129
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 R89 F94 Q97 A135 N136 A137 Q145 F147 W155 H160 R58 F63 Q66 A104 N105 A106 Q114 F116 W124 H129
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding

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Molecular Function
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Biological Process
External links
PDB RCSB:2esl, PDBe:2esl, PDBj:2esl
PDBsum2esl
PubMed20676357
UniProtP45877|PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C (Gene Name=PPIC)

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