Structure of PDB 2cfe Chain A

Receptor sequence
>2cfeA (length=162) Species: 76777 (Malassezia sympodialis) [Search protein sequence]
MSNVFFDITKNGAPLGTIKFKLFDDVVPKTAANFRALCTGEKGFGYAGSH
FHRVIPDFMLQGGDFTAGNGTGGKSIYGAKFADENFQLKHNKPGLLSMAN
AGPNTNGSQFFITTVVTSWLDGKHVVFGEVIDGMNVVKAIEAEGSGSGKP
RSRIEIAKCGVC
3D structure
PDB2cfe Analysis of the cross-reactivity and of the 1.5 A crystal structure of the Malassezia sympodialis Mala s 6 allergen, a member of the cyclophilin pan-allergen family.
ChainA
Resolution1.5 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) R53 F58 Q61 N100 F111 L120 H124
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 ALA A A99 N100 H124 A99 N100 H124
BS02 PRO A R53 Q61 F111 R53 Q61 F111
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0006457 protein folding

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:2cfe, PDBe:2cfe, PDBj:2cfe
PDBsum2cfe
PubMed16483252
UniProtO93970

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