Structure of PDB 4lng Chain B Binding Site BS01

Receptor Information
>4lng Chain B (length=446) Species: 330879 (Aspergillus fumigatus Af293) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HPGIPALFREPPLIHDLLSTETTELQSETVNKCLPLLKGIHNSQKGPFNK
YGIPALQRKDHLEYLYDSLEDYPASFVALDASRPWMVYWALAGLCLLGED
VTRFRERVISTFTAAQNSTGGIGGGHGQMSHVASSYAAVLSIAMVGGEEA
FKLIDRKAMWKWLGKLKQPDGGFTVCEGGEEDVRGAYCAMVVHALLDLPL
ALPPEAEARQNGLETFTDGLPEYLSRCQTYEGGISGSPGSEAHGAYAFCA
LACLCLLGRPEVVVPRYMNIATLLPWLSARQYAPEGGFSGRTNKLVDGCY
SHWVGNCWPLVQAALDGTQPLSSVGNLYSREGLTRYILSCCQCKLGGLRD
KPGKHPDSYHTCYALTGLSTVQYYHYCTDSSVSSKDDFSSAFSWKHDPNF
ASDGQGSDIGVFTENDRLVPFHPIFVIPHKSAEDIRVWFENQSFDL
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain4lng Chain B Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4lng Crystal structures of the fungal pathogen Aspergillus fumigatus protein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design.
Resolution1.905 Å
Binding residue
(original residue number in PDB)		D365 C367 H433
Binding residue
(residue number reindexed from 1)		D297 C299 H360
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H311 R359 K362 D365 C367 Y368 D423 D430 H433
Catalytic site (residue number reindexed from 1) H243 R291 K294 D297 C299 Y300 D350 D357 H360
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:4lng, PDBe:4lng, PDBj:4lng
PDBsum4lng
PubMed24347326
UniProtQ4WPS9

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