Structure of PDB 1n94 Chain A

Receptor sequence
>1n94A (length=315) Species: 10116 (Rattus norvegicus) [Search protein sequence]
FLSLDSPTYVLYRDRAEWADIDPVPQNDGPSPVVQIIYSEKFRDVYDYFR
AVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLRSLQKDLQEEMNY
IIAIIEEQPKNYQVWHHRRVLVEWLKDPSQELEFIADILNQDAKNYHAWQ
HRQWVIQEFRLWDNELQYVDQLLKEDVRNNSVWNQRHFVISNTTGYSDRA
VLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSRYPNLLNQLLDLQP
SHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKE
YWRYIGRSLQSKHSR
3D structure
PDB1n94 Aryl tetrahydropyridine inhibitors of farnesyltransferase: glycine, phenylalanine and histidine derivatives.
ChainA
Resolution3.5 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 HFP A K164 N199 Y200 H201 K110 N145 Y146 H147
BS02 TIN A K164 Y166 Q167 K110 Y112 Q113 PDBbind-CN: -logKd/Ki=8.96,IC50=1.1nM
Gene Ontology
Molecular Function
GO:0008318 protein prenyltransferase activity
Biological Process
GO:0018342 protein prenylation

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:1n94, PDBe:1n94, PDBj:1n94
PDBsum1n94
PubMed12657282
UniProtQ04631|FNTA_RAT Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (Gene Name=Fnta)

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