Structure of PDB 2zir Chain A Binding Site BS01

Receptor Information

>2zir Chain A (length=314) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

FLSLDSPTYVLYRDRAEWADIDPVPQNDGPSPVVQIIYSEKFRDVYDYFR
AVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLRSLQKDLQEEMNY
ITAIIEEQPKNYQVWHHRRVLVEWLKDPSQELEFIADILNQDAKNYHAWQ
HRQWVIQEFRLWDNELQYVDQLLKEDVRNNSVWNQRHFVISNTTGYSDRA
VLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSRYPNLLNQLLDLQP
SHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKE
YWRYIGRSLQSKHS

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

2zir Chain B Residue 902 [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	2zir Synthesis and structure-activity relationships of novel benzofuran farnesyltransferase inhibitors
Resolution	2.4 Å
Binding residue (original residue number in PDB)	K164 Y166
Binding residue (residue number reindexed from 1)	K110 Y112
Annotation score	5

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:0004659	prenyltransferase activity
GO:0004660	protein farnesyltransferase activity
GO:0004661	protein geranylgeranyltransferase activity
GO:0004662	CAAX-protein geranylgeranyltransferase activity
GO:0004663	Rab geranylgeranyltransferase activity
GO:0005515	protein binding
GO:0008017	microtubule binding
GO:0008270	zinc ion binding
GO:0008318	protein prenyltransferase activity
GO:0030971	receptor tyrosine kinase binding
GO:0036094	small molecule binding
GO:0042277	peptide binding
GO:0043014	alpha-tubulin binding
GO:0060090	molecular adaptor activity
GO:1901363	heterocyclic compound binding

	Biological Process
GO:0007167	enzyme-linked receptor protein signaling pathway
GO:0008284	positive regulation of cell population proliferation
GO:0014070	response to organic cyclic compound
GO:0018342	protein prenylation
GO:0018343	protein farnesylation
GO:0018344	protein geranylgeranylation
GO:0034097	response to cytokine
GO:0035022	positive regulation of Rac protein signal transduction
GO:0043066	negative regulation of apoptotic process
GO:0045787	positive regulation of cell cycle
GO:0051770	positive regulation of nitric-oxide synthase biosynthetic process
GO:0051771	negative regulation of nitric-oxide synthase biosynthetic process
GO:0090044	positive regulation of tubulin deacetylation
GO:1904395	positive regulation of skeletal muscle acetylcholine-gated channel clustering

	Cellular Component
GO:0005737	cytoplasm
GO:0005875	microtubule associated complex
GO:0005953	CAAX-protein geranylgeranyltransferase complex
GO:0005965	protein farnesyltransferase complex

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Cellular Component

External links

PDB	RCSB:2zir, PDBe:2zir, PDBj:2zir
PDBsum	2zir
PubMed	19217288
UniProt	Q04631\|FNTA_RAT Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (Gene Name=Fnta)

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