Structure of PDB 4l9p Chain A Binding Site BS01

Receptor Information
>4l9p Chain A (length=335) Species: 330879 (Aspergillus fumigatus Af293) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GKYSSDPEWASIKPIELNDGSDFGAMPLATISYSPEYLEATSYLRAVMAA
NEMSERALRLTGDIISMNPAHYTVWIYRAKILFALGKDLNEEIEWLNKVA
LKHLKNYQIWHHRQVLMSSRAHFPTLPPREQDFLMEMFAQDAKSYHVWTY
RHWLVRHFKLWDHPREIQDVEALLKADVRNNSAWNHRYMLRFGPRDENEF
DAGLHNTTGPSSEKGRLPVVDEDLVDSELQYSQSRILEAPENRSPWSYAR
GVLQAAGRPLSEWKDFARSFVAVKSSHAIEWLADVYAEEDGSEGSAAEAV
KMLTLLKEKYDPIRRNYWEYRIRQITASAAHATEI
Ligand information
Ligand IDFII
InChIInChI=1S/C17H30NO5P/c1-14(2)7-5-8-15(3)9-6-10-16(4)11-12-23-18-17(19)13-24(20,21)22/h7,9,11H,5-6,8,10,12-13H2,1-4H3,(H,18,19)(H2,20,21,22)/b15-9+,16-11+
InChIKeyJAOBYUCYSAOLHS-XGGJEREUSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(NOC\C=C(/C)CC\C=C(/C)CC\C=C(/C)C)CP(=O)(O)O
OpenEye OEToolkits 1.5.0CC(=CCCC(=CCCC(=CCONC(=O)CP(=O)(O)O)C)C)C
OpenEye OEToolkits 1.5.0CC(=CCC/C(=C/CC/C(=C/CONC(=O)CP(=O)(O)O)/C)/C)C
CACTVS 3.341CC(C)=CCC\C(C)=C\CC\C(C)=C\CONC(=O)C[P](O)(O)=O
CACTVS 3.341CC(C)=CCCC(C)=CCCC(C)=CCONC(=O)C[P](O)(O)=O
FormulaC17 H30 N O5 P
Name[(3,7,11-TRIMETHYL-DODECA-2,6,10-TRIENYLOXYCARBAMOYL)-METHYL]-PHOSPHONIC ACID;
FPP ANALOG
ChEMBL
DrugBankDB07771
ZINCZINC000002046984
PDB chain4l9p Chain B Residue 608 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4l9p Crystal structures of the fungal pathogen Aspergillus fumigatus protein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design.
Resolution1.45 Å
Binding residue
(original residue number in PDB)		Y147 H148
Binding residue
(residue number reindexed from 1)		Y145 H146
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) K107
Catalytic site (residue number reindexed from 1) K105
Enzyme Commision number 2.5.1.58: protein farnesyltransferase.
2.5.1.59: protein geranylgeranyltransferase type I.
Gene Ontology
Molecular Function
GO:0004659 prenyltransferase activity
GO:0004660 protein farnesyltransferase activity
GO:0004661 protein geranylgeranyltransferase activity
GO:0004662 CAAX-protein geranylgeranyltransferase activity
GO:0008318 protein prenyltransferase activity
Biological Process
GO:0007323 peptide pheromone maturation
GO:0018342 protein prenylation
GO:0018343 protein farnesylation
Cellular Component
GO:0005737 cytoplasm
GO:0005953 CAAX-protein geranylgeranyltransferase complex
GO:0005965 protein farnesyltransferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4l9p, PDBe:4l9p, PDBj:4l9p
PDBsum4l9p
PubMed24347326
UniProtQ4WP27

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