Structure of PDB 4l9p Chain B

Receptor sequence
>4l9pB (length=452) Species: 330879 (Aspergillus fumigatus Af293) [Search protein sequence]
VHPGIPALFREPPLIHDLLSTETTELQSETVNKCLPLLKGIHNSQKGPFN
KYGIPALQRKDHLEYLYDSLEDYPASFVALDASRPWMVYWALAGLCLLGE
DVTRFRERVISTFTAAQNSTGGIGGGHGQMSHVASSYAAVLSIAMVGGEE
AFKLIDRKAMWKWLGKLKQPDGGFTVCEGGEEDVRGAYCAMVVHALLDLP
LALPPEAEARQNGLETFTDGLPEYLSRCQTYEGGISGSPGSEAHGAYAFC
ALACLCLLGRPEVVVPRYMNIATLLPWLSARQYAPEGGFSGRTNKLVDGC
YSHWVGNCWPLVQAALDGTQPLAGPKRSSVGNLYSREGLTRYILSCCQCK
LGGLRDKPGKHPDSYHTCYALTGLSTVQYYHYCTDSSVSSKDDFSSAFSW
KHDPNFASDGQGSDIGVFTENDRLVPFHPIFVIPHKSAEDIRVWFENQSF
DL
3D structure
PDB4l9p Crystal structures of the fungal pathogen Aspergillus fumigatus protein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design.
ChainB
Resolution1.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide B W153 H199 R252 Y432 H433 W86 H132 R185 Y365 H366
BS02 ZN B D365 C367 H433 D298 C300 H366
BS03 FII B R252 Y255 H311 A313 Y314 R359 K362 Y368 W371 R185 Y188 H244 A246 Y247 R292 K295 Y301 W304
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:4l9p, PDBe:4l9p, PDBj:4l9p
PDBsum4l9p
PubMed24347326
UniProtQ4WPS9

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