Structure of PDB 4l9p Chain B Binding Site BS01

Receptor Information

>4l9p Chain B (length=452) Species: 330879 (Aspergillus fumigatus Af293)

VHPGIPALFREPPLIHDLLSTETTELQSETVNKCLPLLKGIHNSQKGPFN
KYGIPALQRKDHLEYLYDSLEDYPASFVALDASRPWMVYWALAGLCLLGE
DVTRFRERVISTFTAAQNSTGGIGGGHGQMSHVASSYAAVLSIAMVGGEE
AFKLIDRKAMWKWLGKLKQPDGGFTVCEGGEEDVRGAYCAMVVHALLDLP
LALPPEAEARQNGLETFTDGLPEYLSRCQTYEGGISGSPGSEAHGAYAFC
ALACLCLLGRPEVVVPRYMNIATLLPWLSARQYAPEGGFSGRTNKLVDGC
YSHWVGNCWPLVQAALDGTQPLAGPKRSSVGNLYSREGLTRYILSCCQCK
LGGLRDKPGKHPDSYHTCYALTGLSTVQYYHYCTDSSVSSKDDFSSAFSW
KHDPNFASDGQGSDIGVFTENDRLVPFHPIFVIPHKSAEDIRVWFENQSF
DL

Ligand information

>4l9p Chain C (length=5)

KCVVM

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4l9p Crystal structures of the fungal pathogen Aspergillus fumigatus protein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design.
• Resolution: 1.45 Å
• Binding residue (original residue number in PDB): W153 H199 R252 Y432 H433
• Binding residue (residue number reindexed from 1): W86 H132 R185 Y365 H366

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

External links

• PDB: RCSB:4l9p, PDBe:4l9p, PDBj:4l9p
• PDBsum: 4l9p
• PubMed: 24347326
• UniProt: Q4WPS9