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Receptor Information

>4gtr Chain B (length=403) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

EPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPR
LVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQ
IVATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYN
VINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPD
LFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKERSLNL
KSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGD
PALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGL
SIAQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFLQKPV
PGF

Ligand ID

7TR

InChI

InChI=1S/C34H38N6O5S/c1-5-38(6-2)34(41)45-31-10-7-25(8-11-31)18-28-22-39(23-29-20-36-24-37(29)3)33-16-9-26(19-35)17-27(33)21-40(28)46(42,43)32-14-12-30(44-4)13-15-32/h7-17,20,24,28H,5-6,18,21-23H2,1-4H3/t28-/m1/s1

InChIKey

IQZAPWUUBMPSLO-MUUNZHRXSA-N

SMILES

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

Formula

C34 H38 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 diethylcarbamate

PDB chain

4gtr Chain B Residue 502 [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	4gtr Development of Selective, Potent RabGGTase Inhibitors
Resolution	2.2 Å
Binding residue (original residue number in PDB)	L96 W102 Y105 W106 D297 D359 Y361 H362 Y365
Binding residue (residue number reindexed from 1)	L76 W82 Y85 W86 D277 D339 Y341 H342 Y345
Annotation score	1
Binding affinity	PDBbind-CN: -logKd/Ki=8.30,IC50<5nM

Catalytic site (original residue number in PDB)	H248 R291 K294 D297 C299 Y300 D352 D359 H362
Catalytic site (residue number reindexed from 1)	H228 R271 K274 D277 C279 Y280 D332 D339 H342
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:4gtr, PDBe:4gtr, PDBj:4gtr
PDBsum	4gtr
PubMed	22963166
UniProt	Q02293\|FNTB_RAT Protein farnesyltransferase subunit beta (Gene Name=Fntb)

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Structure of PDB 4gtr Chain B Binding Site BS02