Structure of PDB 4l9p Chain B Binding Site BS02

Receptor Information
>4l9p Chain B (length=452) 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
YSHWVGNCWPLVQAALDGTQPLAGPKRSSVGNLYSREGLTRYILSCCQCK
LGGLRDKPGKHPDSYHTCYALTGLSTVQYYHYCTDSSVSSKDDFSSAFSW
KHDPNFASDGQGSDIGVFTENDRLVPFHPIFVIPHKSAEDIRVWFENQSF
DL
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 chain4l9p Chain B Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
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)		D365 C367 H433
Binding residue
(residue number reindexed from 1)		D298 C300 H366
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) H244 R292 K295 D298 C300 Y301 D356 D363 H366
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4l9p, PDBe:4l9p, PDBj:4l9p
PDBsum4l9p
PubMed24347326
UniProtQ4WPS9

[Back to BioLiP]