Structure of PDB 1qbq Chain A

Receptor sequence
>1qbqA (length=312) Species: 10116 (Rattus norvegicus) [Search protein sequence]
FLSLDSPTYVLYRDRAEWADIDPVPQNDGPSPVVQIIYSEKFRDVYDYFR
AVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLRSLQKDLQEEMNY
ITAIIEEQPKNYQVWHHRRVLVEWLKDPSQELEFIADILNQDAKNYHAWQ
HRQWVIQEFRLWDNELQYVDQLLKEDVRNNSVWNQRHFVISNTTGYSDRA
VLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSRYPNLLNQLLDLQP
SHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKE
YWRYIGRSLQSK
3D structure
PDB1qbq Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K164
Catalytic site (residue number reindexed from 1) K110
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 peptide A K164 Y166 K110 Y112
Gene Ontology
Molecular Function
GO:0008318 protein prenyltransferase activity
Biological Process
GO:0018342 protein prenylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1qbq, PDBe:1qbq, PDBj:1qbq
PDBsum1qbq
PubMed9843427
UniProtQ04631|FNTA_RAT Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (Gene Name=Fnta)

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