Structure of PDB 4lng Chain B

Receptor sequence
>4lngB (length=446) Species: 330879 (Aspergillus fumigatus Af293) [Search protein sequence]
HPGIPALFREPPLIHDLLSTETTELQSETVNKCLPLLKGIHNSQKGPFNK
YGIPALQRKDHLEYLYDSLEDYPASFVALDASRPWMVYWALAGLCLLGED
VTRFRERVISTFTAAQNSTGGIGGGHGQMSHVASSYAAVLSIAMVGGEEA
FKLIDRKAMWKWLGKLKQPDGGFTVCEGGEEDVRGAYCAMVVHALLDLPL
ALPPEAEARQNGLETFTDGLPEYLSRCQTYEGGISGSPGSEAHGAYAFCA
LACLCLLGRPEVVVPRYMNIATLLPWLSARQYAPEGGFSGRTNKLVDGCY
SHWVGNCWPLVQAALDGTQPLSSVGNLYSREGLTRYILSCCQCKLGGLRD
KPGKHPDSYHTCYALTGLSTVQYYHYCTDSSVSSKDDFSSAFSWKHDPNF
ASDGQGSDIGVFTENDRLVPFHPIFVIPHKSAEDIRVWFENQSFDL
3D structure
PDB4lng Crystal structures of the fungal pathogen Aspergillus fumigatus protein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design.
ChainB
Resolution1.905 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
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 ZN B D365 C367 H433 D297 C299 H360
BS02 JAN B W157 D365 C367 D430 Y432 H433 W89 D297 C299 D357 Y359 H360 PDBbind-CN: -logKd/Ki=5.62,IC50=2400nM
BS03 FPP B R252 H311 R359 K362 Y368 W371 R184 H243 R291 K294 Y300 W303
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:4lng, PDBe:4lng, PDBj:4lng
PDBsum4lng
PubMed24347326
UniProtQ4WPS9

[Back to BioLiP]