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Receptor Information

>4gtm Chain B (length=405) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

WSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLV
PRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPI
PQIVATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTEEA
YNVINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIIT
PDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKERSL
NLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQ
GDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLS
GLSIAQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFLQK
PVPGF

Ligand ID

7TM

InChI

InChI=1S/C36H42N6O5S/c1-4-5-6-7-18-39-36(43)47-33-11-8-27(9-12-33)20-30-24-41(25-31-22-38-26-40(31)2)35-17-10-28(21-37)19-29(35)23-42(30)48(44,45)34-15-13-32(46-3)14-16-34/h8-17,19,22,26,30H,4-7,18,20,23-25H2,1-3H3,(H,39,43)/t30-/m1/s1

InChIKey

HGCSBLLHUYZWLK-SSEXGKCCSA-N

SMILES

Software	SMILES
CACTVS 3.370	CCCCCCNC(=O)Oc1ccc(C[CH]2CN(Cc3cncn3C)c4ccc(cc4CN2[S](=O)(=O)c5ccc(OC)cc5)C#N)cc1
CACTVS 3.370	CCCCCCNC(=O)Oc1ccc(C[C@@H]2CN(Cc3cncn3C)c4ccc(cc4CN2[S](=O)(=O)c5ccc(OC)cc5)C#N)cc1
OpenEye OEToolkits 1.7.6	CCCCCCNC(=O)Oc1ccc(cc1)CC2CN(c3ccc(cc3CN2S(=O)(=O)c4ccc(cc4)OC)C#N)Cc5cncn5C
OpenEye OEToolkits 1.7.6	CCCCCCNC(=O)Oc1ccc(cc1)C[C@@H]2CN(c3ccc(cc3CN2S(=O)(=O)c4ccc(cc4)OC)C#N)Cc5cncn5C
ACDLabs 12.01	O=C(Oc1ccc(cc1)CC2N(Cc4cc(C#N)ccc4N(C2)Cc3cncn3C)S(=O)(=O)c5ccc(OC)cc5)NCCCCCC

Formula

C36 H42 N6 O5 S

Name

4-({(3R)-7-cyano-4-[(4-methoxyphenyl)sulfonyl]-1-[(1-methyl-1H-imidazol-5-yl)methyl]-2,3,4,5-tetrahydro-1H-1,4-benzodiazepin-3-yl}methyl)phenyl hexylcarbamate

PDB chain

4gtm Chain B Residue 503 [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	4gtm Development of Selective, Potent RabGGTase Inhibitors
Resolution	2.2 Å
Binding residue (original residue number in PDB)	L96 A98 S99 W102 A151 P152 D297 D359 Y361 H362
Binding residue (residue number reindexed from 1)	L78 A80 S81 W84 A133 P134 D279 D341 Y343 H344
Annotation score	1
Binding affinity	MOAD: ic50=9.2nM PDBbind-CN: -logKd/Ki=8.04,IC50=9.2nM

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.

	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:4gtm, PDBe:4gtm, PDBj:4gtm
PDBsum	4gtm
PubMed	22963166
UniProt	Q02293\|FNTB_RAT Protein farnesyltransferase subunit beta (Gene Name=Fntb)

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Structure of PDB 4gtm Chain B Binding Site BS03