Structure of PDB 2cfe Chain A Binding Site BS02

Receptor Information

>2cfe Chain A (length=162) Species: 76777 (Malassezia sympodialis)

MSNVFFDITKNGAPLGTIKFKLFDDVVPKTAANFRALCTGEKGFGYAGSH
FHRVIPDFMLQGGDFTAGNGTGGKSIYGAKFADENFQLKHNKPGLLSMAN
AGPNTNGSQFFITTVVTSWLDGKHVVFGEVIDGMNVVKAIEAEGSGSGKP
RSRIEIAKCGVC

Ligand information

• Ligand ID: PRO
• InChI: InChI=1S/C5H9NO2/c7-5(8)4-2-1-3-6-4/h4,6H,1-3H2,(H,7,8)/t4-/m0/s1
• InChIKey: ONIBWKKTOPOVIA-BYPYZUCNSA-N
• SMILES:
  OpenEye OEToolkits 1.5.0: C1C[C@H](NC1)C(=O)O
  CACTVS 3.341: OC(=O)[C@@H]1CCCN1
  CACTVS 3.341: OC(=O)[CH]1CCCN1
  OpenEye OEToolkits 1.5.0: C1CC(NC1)C(=O)O
  ACDLabs 10.04: O=C(O)C1NCCC1
• Formula: C5 H9 N O2
• Name: PROLINE
• ChEMBL: CHEMBL54922
• DrugBank: DB00172
• ZINC: ZINC000000895360
• PDB chain: 2cfe Chain A Residue 1162

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2cfe 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.
• Resolution: 1.5 Å
• Binding residue (original residue number in PDB): R53 Q61 F111
• Binding residue (residue number reindexed from 1): R53 Q61 F111
• Annotation score: 1

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.

Gene Ontology

Molecular Function

• GO:0003755 peptidyl-prolyl cis-trans isomerase activity

Biological Process

• GO:0000413 protein peptidyl-prolyl isomerization
• GO:0006457 protein folding

External links

• PDB: RCSB:2cfe, PDBe:2cfe, PDBj:2cfe
• PDBsum: 2cfe
• PubMed: 16483252
• UniProt: O93970