Structure of PDB 1qbq Chain A Binding Site BS01
Receptor Information
>1qbq Chain A (length=312) Species:
10116
(Rattus norvegicus) [
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FLSLDSPTYVLYRDRAEWADIDPVPQNDGPSPVVQIIYSEKFRDVYDYFR
AVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLRSLQKDLQEEMNY
ITAIIEEQPKNYQVWHHRRVLVEWLKDPSQELEFIADILNQDAKNYHAWQ
HRQWVIQEFRLWDNELQYVDQLLKEDVRNNSVWNQRHFVISNTTGYSDRA
VLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSRYPNLLNQLLDLQP
SHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKE
YWRYIGRSLQSK
Ligand information
>1qbq Chain P (length=4) [
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CVIM
Receptor-Ligand Complex Structure
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PDB
1qbq
Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue
Resolution
2.4 Å
Binding residue
(original residue number in PDB)
K164 Y166
Binding residue
(residue number reindexed from 1)
K110 Y112
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.
Gene Ontology
Molecular Function
GO:0008318
protein prenyltransferase activity
Biological Process
GO:0018342
protein prenylation
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Molecular Function
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Biological Process
External links
PDB
RCSB:1qbq
,
PDBe:1qbq
,
PDBj:1qbq
PDBsum
1qbq
PubMed
9843427
UniProt
Q04631
|FNTA_RAT Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (Gene Name=Fnta)
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