Structure of PDB 4gtq Chain B

Receptor sequence
>4gtqB (length=405) Species: 10116 (Rattus norvegicus) [Search protein sequence]
WSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLV
PRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPI
PQIVATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTEEA
YNVINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIIT
PDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKERSL
NLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQ
GDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLS
GLSIAQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFLQK
PVPGF
3D structure
PDB4gtq Development of Selective, Potent RabGGTase Inhibitors
ChainB
Resolution2.6 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) H230 R273 K276 D279 C281 Y282 D334 D341 H344
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 ZN B D297 C299 H362 D279 C281 H344
BS02 FPP B R202 H248 G250 Y251 R291 K294 Y300 W303 R184 H230 G232 Y233 R273 K276 Y282 W285
BS03 7TQ B L96 A98 S99 W102 A151 P152 D297 D359 Y361 H362 L78 A80 S81 W84 A133 P134 D279 D341 Y343 H344 PDBbind-CN: -logKd/Ki=8.30,IC50<5nM
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:4gtq, PDBe:4gtq, PDBj:4gtq
PDBsum4gtq
PubMed22963166
UniProtQ02293|FNTB_RAT Protein farnesyltransferase subunit beta (Gene Name=Fntb)

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