Structure of PDB 1jcs Chain B

Receptor sequence
>1jcsB (length=407) Species: 10116 (Rattus norvegicus) [Search protein sequence]
PVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNH
LVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDE
PIPQIVATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTE
EAYNVINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNI
ITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKER
SLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALH
AQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYC
LSGLSIAQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFL
QKPVPGF
3D structure
PDB1jcs The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H248 R291 K294 D297 C299 Y300 D352 D359 H362
Catalytic site (residue number reindexed from 1) H232 R275 K278 D281 C283 Y284 D336 D343 H346
Enzyme Commision number 2.5.1.58: protein farnesyltransferase.
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 B W102 W106 R202 K356 H362 W86 W90 R186 K340 H346
BS02 ZN B D297 C299 H362 D281 C283 H346
BS03 FII B H248 G250 R291 K294 Y300 W303 H232 G234 R275 K278 Y284 W287
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004311 farnesyltranstransferase activity
GO:0004659 prenyltransferase activity
GO:0004660 protein farnesyltransferase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0008318 protein prenyltransferase activity
GO:0042277 peptide binding
GO:0046872 metal ion binding
Biological Process
GO:0006629 lipid metabolic process
GO:0008283 cell population proliferation
GO:0008284 positive regulation of cell population proliferation
GO:0008285 negative regulation of cell population proliferation
GO:0014070 response to organic cyclic compound
GO:0018343 protein farnesylation
GO:0034097 response to cytokine
GO:0042060 wound healing
GO:0045787 positive regulation of cell cycle
GO:0048144 fibroblast proliferation
GO:0048145 regulation of fibroblast proliferation
GO:0048146 positive regulation of fibroblast proliferation
GO:0051770 positive regulation of nitric-oxide synthase biosynthetic process
Cellular Component
GO:0005875 microtubule associated complex
GO:0005965 protein farnesyltransferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1jcs, PDBe:1jcs, PDBj:1jcs
PDBsum1jcs
PubMed11687658
UniProtQ02293|FNTB_RAT Protein farnesyltransferase subunit beta (Gene Name=Fntb)

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