Structure of PDB 4lnb Chain B Binding Site BS03

Receptor Information
>4lnb Chain B (length=447) Species: 330879 (Aspergillus fumigatus Af293) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VHPGIPALFREPPLIHDLLSTETTELQSETVNKCLPLLKGIHNSQKGPFN
KYGIPALQRKDHLEYLYDSLEDYPASFVALDASRPWMVYWALAGLCLLGE
DVTRFRERVISTFTAAQNSTGGIGGGHGQMSHVASSYAAVLSIAMVGGEE
AFKLIDRKAMWKWLGKLKQPDGGFTVCEGGEEDVRGAYCAMVVHALLDLP
LALPPEAEARQNGLETFTDGLPEYLSRCQTYEGGISGSPGSEAHGAYAFC
ALACLCLLGRPEVVVPRYMNIATLLPWLSARQYAPEGGFSGRTNKLVDGC
YSHWVGNCWPLVQAALDGTQPLARSSVGNLYSREGLTRYILSCCQCKLGG
LRDKPGKHPDSYHTCYALTGLSTVQYYHYCTDSSVSSKFSSAFSWKHDPN
FASDGQGSDIGVFTENDRLVPFHPIFVIPHKSAEDIRVWFENQSFDL
Ligand information
Ligand IDED5
InChIInChI=1S/C32H42N6O4S/c1-25-8-6-7-9-30(25)43(40,41)38(22-27-14-16-36(17-15-27)31(39)42-32(2,3)4)19-18-37(23-29-21-34-24-35(29)5)28-12-10-26(20-33)11-13-28/h6-13,21,24,27H,14-19,22-23H2,1-5H3
InChIKeyCHEKEDNUVFBGCF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cn1cncc1CN(CCN(CC2CCN(CC2)C(=O)OC(C)(C)C)[S](=O)(=O)c3ccccc3C)c4ccc(cc4)C#N
OpenEye OEToolkits 1.5.0Cc1ccccc1S(=O)(=O)N(CCN(Cc2cncn2C)c3ccc(cc3)C#N)CC4CCN(CC4)C(=O)OC(C)(C)C
ACDLabs 10.04O=C(OC(C)(C)C)N1CCC(CC1)CN(S(=O)(=O)c2ccccc2C)CCN(c3ccc(C#N)cc3)Cc4cncn4C
OpenEye OEToolkits 1.5.0Cc1ccccc1S(=O)(=O)[N@](CC[N@@](Cc2cncn2C)c3ccc(cc3)C#N)CC4CCN(CC4)C(=O)OC(C)(C)C
FormulaC32 H42 N6 O4 S
Nametert-butyl 4-({(2-{(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino}ethyl)[(2-methylphenyl)sulfonyl]amino}methyl)piperidine-1-carboxylate
ChEMBL
DrugBank
ZINCZINC000039187973
PDB chain4lnb Chain B Residue 603 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4lnb Crystal structures of the fungal pathogen Aspergillus fumigatus protein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design.
Resolution1.752 Å
Binding residue
(original residue number in PDB)		A168 L169 R274 D387 C389 D452 Y454 H455
Binding residue
(residue number reindexed from 1)		A79 L80 R185 D298 C300 D360 Y362 H363
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=6.56,IC50=275nM
Enzymatic activity
Catalytic site (original residue number in PDB) H333 R381 K384 D387 C389 Y390 D445 D452 H455
Catalytic site (residue number reindexed from 1) H244 R292 K295 D298 C300 Y301 D353 D360 H363
Enzyme Commision number 2.5.1.58: protein farnesyltransferase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004659 prenyltransferase activity
GO:0004660 protein farnesyltransferase activity
GO:0008270 zinc ion binding
GO:0008318 protein prenyltransferase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0018343 protein farnesylation
GO:0097354 prenylation
Cellular Component
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:4lnb, PDBe:4lnb, PDBj:4lnb
PDBsum4lnb
PubMed24347326
UniProtQ4WPS9

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