Structure of PDB 3pmp Chain B

Receptor sequence
>3pmpB (length=163) Species: 153609 (Moniliophthora perniciosa) [Search protein sequence]
AMANVFFNISINDKPEGRIVFKLYDEAVPKTAKNFRELATGQHGFGYKDS
IFHRVIPQFMLQGGDFTRHNGTGGKSIYGEKFADENFQVKHTKPGLLSMA
NAGANTNGSQFFITTVPTSWLDGKHVVFGEVIEGLDIVRKVEGKGSASGK
TNATIKITDCGTV
3D structure
PDB3pmp Crystal Structure of Cyclophilin A from Moniliophthora perniciosa
ChainB
Resolution1.47 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) R54 F59 Q62 N101 F112 L121 H125
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 B R53 F58 Q61 G70 A99 N100 A101 Q109 F111 W119 H124 R54 F59 Q62 G71 A100 N101 A102 Q110 F112 W120 H125
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:3pmp, PDBe:3pmp, PDBj:3pmp
PDBsum3pmp
PubMed
UniProtE3P6K5

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