BioLiP

Receptor Information

>2zis 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 ID

NH8

InChI

InChI=1S/C27H17N5O4/c1-31-16-30-15-24(31)27(33,21-7-5-17(13-28)6-8-21)25-11-20-10-22(32(34)35)12-23(26(20)36-25)19-4-2-3-18(9-19)14-29/h2-12,15-16,33H,1H3/t27-/m0/s1

InChIKey

NYEPLLLECMESPU-MHZLTWQESA-N

SMILES

Software	SMILES
CACTVS 3.341	Cn1cncc1[C](O)(c2oc3c(c2)cc(cc3c4cccc(c4)C#N)[N+]([O-])=O)c5ccc(cc5)C#N
OpenEye OEToolkits 1.5.0	Cn1cncc1[C@@](c2ccc(cc2)C#N)(c3cc4cc(cc(c4o3)c5cccc(c5)C#N)[N+](=O)[O-])O
ACDLabs 10.04	N#Cc1ccc(cc1)C(O)(c2cncn2C)c4oc3c(cc(cc3c4)[N+]([O-])=O)c5cccc(C#N)c5
OpenEye OEToolkits 1.5.0	Cn1cncc1C(c2ccc(cc2)C#N)(c3cc4cc(cc(c4o3)c5cccc(c5)C#N)[N+](=O)[O-])O
CACTVS 3.341	Cn1cncc1[C@](O)(c2oc3c(c2)cc(cc3c4cccc(c4)C#N)[N+]([O-])=O)c5ccc(cc5)C#N

Formula

C27 H17 N5 O4

Name

3-{2-[(S)-(4-cyanophenyl)(hydroxy)(1-methyl-1H-imidazol-5-yl)methyl]-5-nitro-1-benzofuran-7-yl}benzonitrile

PDB chain

2zis Chain B Residue 903 [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	2zis Synthesis and structure-activity relationships of novel benzofuran farnesyltransferase inhibitors
Resolution	2.6 Å
Binding residue (original residue number in PDB)	L96 W102 W106 R202 D297 C299 D359 Y361 H362
Binding residue (residue number reindexed from 1)	L75 W81 W85 R181 D276 C278 D338 Y340 H341
Annotation score	1
Binding affinity	PDBbind-CN: -logKd/Ki=8.55,IC50=2.8nM

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.

	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

PDB	RCSB:2zis, PDBe:2zis, PDBj:2zis
PDBsum	2zis
PubMed	19217288
UniProt	Q02293\|FNTB_RAT Protein farnesyltransferase subunit beta (Gene Name=Fntb)

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Structure of PDB 2zis Chain B Binding Site BS03