Structure of PDB 4lnb Chain B

Receptor sequence
>4lnbB (length=447) Species: 330879 (Aspergillus fumigatus Af293) [Search protein sequence]
VHPGIPALFREPPLIHDLLSTETTELQSETVNKCLPLLKGIHNSQKGPFN
KYGIPALQRKDHLEYLYDSLEDYPASFVALDASRPWMVYWALAGLCLLGE
DVTRFRERVISTFTAAQNSTGGIGGGHGQMSHVASSYAAVLSIAMVGGEE
AFKLIDRKAMWKWLGKLKQPDGGFTVCEGGEEDVRGAYCAMVVHALLDLP
LALPPEAEARQNGLETFTDGLPEYLSRCQTYEGGISGSPGSEAHGAYAFC
ALACLCLLGRPEVVVPRYMNIATLLPWLSARQYAPEGGFSGRTNKLVDGC
YSHWVGNCWPLVQAALDGTQPLARSSVGNLYSREGLTRYILSCCQCKLGG
LRDKPGKHPDSYHTCYALTGLSTVQYYHYCTDSSVSSKFSSAFSWKHDPN
FASDGQGSDIGVFTENDRLVPFHPIFVIPHKSAEDIRVWFENQSFDL
3D structure
PDB4lnb Crystal structures of the fungal pathogen Aspergillus fumigatus protein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design.
ChainB
Resolution1.752 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) 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.
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 FPP B R274 Y277 H333 A335 R381 K384 Y390 W393 R185 Y188 H244 A246 R292 K295 Y301 W304
BS02 ZN B D387 C389 H455 D298 C300 H363
BS03 ED5 B A168 L169 R274 D387 C389 D452 Y454 H455 A79 L80 R185 D298 C300 D360 Y362 H363 PDBbind-CN: -logKd/Ki=6.56,IC50=275nM
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:4lnb, PDBe:4lnb, PDBj:4lnb
PDBsum4lnb
PubMed24347326
UniProtQ4WPS9

[Back to BioLiP]