Structure of PDB 3e34 Chain B Binding Site BS03

Receptor Information

>3e34 Chain B (length=407) Species: 10116 (Rattus norvegicus)

PVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNH
LVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDE
PIPQIVATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTE
EAYNVINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNI
ITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKER
SLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALH
AQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYC
LSGLSIAQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFL
QKPVPGF

Ligand information

• Ligand ID: ED1
• InChI: InChI=1S/C40H48N6O6S/c1-40(2,3)52-39(49)44-20-18-32(19-21-44)27-46(23-22-45(28-35-26-42-29-43(35)4)34-15-12-31(25-41)13-16-34)53(50,51)37-11-6-5-10-36(37)33-9-7-8-30(24-33)14-17-38(47)48/h5-13,15-16,24,26,29,32H,14,17-23,27-28H2,1-4H3,(H,47,48)
• InChIKey: IQLSFMXNAXIRFW-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: Cn1cncc1CN(CCN(CC2CCN(CC2)C(=O)OC(C)(C)C)[S](=O)(=O)c3ccccc3c4cccc(CCC(O)=O)c4)c5ccc(cc5)C#N
  OpenEye OEToolkits 1.5.0: CC(C)(C)OC(=O)N1CCC(CC1)CN(CCN(Cc2cncn2C)c3ccc(cc3)C#N)S(=O)(=O)c4ccccc4c5cccc(c5)CCC(=O)O
  OpenEye OEToolkits 1.5.0: CC(C)(C)OC(=O)N1CCC(CC1)C[N@@](CC[N@@](Cc2cncn2C)c3ccc(cc3)C#N)S(=O)(=O)c4ccccc4c5cccc(c5)CCC(=O)O
  ACDLabs 10.04: O=C(O)CCc1cccc(c1)c2ccccc2S(=O)(=O)N(CC3CCN(C(=O)OC(C)(C)C)CC3)CCN(c4ccc(C#N)cc4)Cc5cncn5C
• Formula: C40 H48 N6 O6 S
• Name: 3-{2'-[{[1-(tert-butoxycarbonyl)piperidin-4-yl]methyl}(2-{(4-cyanophenyl)[(1-methyl-1H-imidazol-5-yl)methyl]amino}ethyl)sulfamoyl]biphenyl-3-yl}propanoic acid
• ZINC: ZINC000058632712
• PDB chain: 3e34 Chain B Residue 1003

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3e34 Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase.
• Resolution: 2.05 Å
• Binding residue (original residue number in PDB): L96 W102 A151 D297 W303 D359 Y361 H362
• Binding residue (residue number reindexed from 1): L80 W86 A135 D281 W287 D343 Y345 H346
• Annotation score: 1

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): H232 R275 K278 D281 C283 Y284 D336 D343 H346
• 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

External links

• PDB: RCSB:3e34, PDBe:3e34, PDBj:3e34
• PDBsum: 3e34
• PubMed: 19246009
• UniProt: Q02293|FNTB_RAT Protein farnesyltransferase subunit beta (Gene Name=Fntb)