Structure of PDB 4l9p Chain A

Receptor sequence

>4l9pA (length=335) Species: 330879 (Aspergillus fumigatus Af293)

GKYSSDPEWASIKPIELNDGSDFGAMPLATISYSPEYLEATSYLRAVMAA
NEMSERALRLTGDIISMNPAHYTVWIYRAKILFALGKDLNEEIEWLNKVA
LKHLKNYQIWHHRQVLMSSRAHFPTLPPREQDFLMEMFAQDAKSYHVWTY
RHWLVRHFKLWDHPREIQDVEALLKADVRNNSAWNHRYMLRFGPRDENEF
DAGLHNTTGPSSEKGRLPVVDEDLVDSELQYSQSRILEAPENRSPWSYAR
GVLQAAGRPLSEWKDFARSFVAVKSSHAIEWLADVYAEEDGSEGSAAEAV
KMLTLLKEKYDPIRRNYWEYRIRQITASAAHATEI

3D structure

• PDB: 4l9p Crystal structures of the fungal pathogen Aspergillus fumigatus protein farnesyltransferase complexed with substrates and inhibitors reveal features for antifungal drug design.
• Chain: A
• Resolution: 1.45 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K107
• Catalytic site (residue number reindexed from 1): K105
• Enzyme Commision number: 2.5.1.58: protein farnesyltransferase.
  2.5.1.59: protein geranylgeranyltransferase type I.

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	FII	A	Y147 H148	Y145 H146

Gene Ontology

Molecular Function

• GO:0004659 prenyltransferase activity
• GO:0004660 protein farnesyltransferase activity
• GO:0004661 protein geranylgeranyltransferase activity
• GO:0004662 CAAX-protein geranylgeranyltransferase activity
• GO:0008318 protein prenyltransferase activity

Biological Process

• GO:0007323 peptide pheromone maturation
• GO:0018342 protein prenylation
• GO:0018343 protein farnesylation

Cellular Component

• GO:0005737 cytoplasm
• GO:0005953 CAAX-protein geranylgeranyltransferase complex
• GO:0005965 protein farnesyltransferase complex

External links

• PDB: RCSB:4l9p, PDBe:4l9p, PDBj:4l9p
• PDBsum: 4l9p
• PubMed: 24347326
• UniProt: Q4WP27