Structure of PDB 1ft2 Chain B Binding Site BS02

Receptor Information

>1ft2 Chain B (length=401) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

PLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRL
VLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQI
VATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYNV
INREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDL
FEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKERSLNLK
SLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDP
ALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLS
IAQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFLQKPVP
G

Ligand information

Ligand ID

FPP

InChI

InChI=1S/C15H28O7P2/c1-13(2)7-5-8-14(3)9-6-10-15(4)11-12-21-24(19,20)22-23(16,17)18/h7,9,11H,5-6,8,10,12H2,1-4H3,(H,19,20)(H2,16,17,18)/b14-9+,15-11+

InChIKey

VWFJDQUYCIWHTN-YFVJMOTDSA-N

SMILES

Software	SMILES
CACTVS 3.341	CC(C)=CCCC(C)=CCCC(C)=CCO[P](O)(=O)O[P](O)(O)=O
ACDLabs 10.04	O=P(OC/C=C(/CC\C=C(/C)CC\C=C(/C)C)C)(OP(=O)(O)O)O
OpenEye OEToolkits 1.5.0	CC(=CCC/C(=C/CC/C(=C/CO[P@@](=O)(O)OP(=O)(O)O)/C)/C)C
CACTVS 3.341	CC(C)=CCCC(/C)=C/CCC(/C)=C/CO[P@](O)(=O)O[P](O)(O)=O
OpenEye OEToolkits 1.5.0	CC(=CCCC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C)C

Formula

C15 H28 O7 P2

Name

FARNESYL DIPHOSPHATE

PDB chain

1ft2 Chain B Residue 1 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1ft2 Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate.
Resolution	3.4 Å
Binding residue (original residue number in PDB)	H248 C254 R291 K294 Y300
Binding residue (residue number reindexed from 1)	H227 C233 R270 K273 Y279
Annotation score	5

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)	H227 R270 K273 D276 C278 Y279 D331 D338 H341
Enzyme Commision number	2.5.1.58: protein farnesyltransferase.

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:1ft2, PDBe:1ft2, PDBj:1ft2
PDBsum	1ft2
PubMed	9657673
UniProt	Q02293\|FNTB_RAT Protein farnesyltransferase subunit beta (Gene Name=Fntb)

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