Structure of PDB 1o1t Chain B Binding Site BS03

Receptor Information

>1o1t Chain B (length=401) Species: 10116 (Rattus norvegicus)

LYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLV
LQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIV
ATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYNVI
NREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLF
EGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKERSLNLKS
LLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPA
LSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSI
AQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFLQKPVPG
F

Ligand information

• Ligand ID: 2NH
• InChI: InChI=1S/C36H62N4O6S2/c1-11-27(8)32(35(44)38-29(36(45)46)19-20-47-10)40-34(43)31(24(4)5)39-33(42)30(37-28(9)41)22-48-21-18-26(7)17-13-16-25(6)15-12-14-23(2)3/h14,16,18,24,27,29-32H,11-13,15,17,19-22H2,1-10H3,(H,37,41)(H,38,44)(H,39,42)(H,40,43)(H,45,46)/b25-16+,26-18+/t27-,29-,30-,31-,32-/m0/s1
• InChIKey: LZZSZMJTHYOSLN-UNXIWMFYSA-N
• SMILES:
  CACTVS 3.341: CC[C@H](C)[C@H](NC(=O)[C@@H](NC(=O)[C@H](CSC\C=C(/C)CC\C=C(/C)CCC=C(C)C)NC(C)=O)C(C)C)C(=O)N[C@@H](CCSC)C(O)=O
  OpenEye OEToolkits 1.5.0: CCC(C)C(C(=O)NC(CCSC)C(=O)O)NC(=O)C(C(C)C)NC(=O)C(CSCC=C(C)CCC=C(C)CCC=C(C)C)NC(=O)C
  OpenEye OEToolkits 1.5.0: CC[C@H](C)[C@@H](C(=O)N[C@@H](CCSC)C(=O)O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CSC\C=C(/C)\CC\C=C(/C)\CCC=C(C)C)NC(=O)C
  ACDLabs 10.04: O=C(NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)O)CCSC)C(C)CC)C(C)C)CSC\C=C(/C)CC\C=C(/C)CC\C=C(/C)C)C
  CACTVS 3.341: CC[CH](C)[CH](NC(=O)[CH](NC(=O)[CH](CSCC=C(C)CCC=C(C)CCC=C(C)C)NC(C)=O)C(C)C)C(=O)N[CH](CCSC)C(O)=O
• Formula: C36 H62 N4 O6 S2
• Name: N-ACETYL-S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL]-L-CYSTEINYL-D-VALYL-L-ISOLEUCYL-L-METHIONINE
• ZINC: ZINC000024638927
• PDB chain: 1o1t Chain B Residue 3001

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1o1t Biochemical and Structural Studies with Prenyl Diphosphate Analogues Provide Insights into Isoprenoid Recognition by Protein Farnesyl Transferase
• Resolution: 2.1 Å
• Binding residue (original residue number in PDB): W102 P152 R202 Y205 G250 C299 Y300 Y361
• Binding residue (residue number reindexed from 1): W80 P130 R180 Y183 G228 C277 Y278 Y339
• 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): H226 R269 K272 D275 C277 Y278 D330 D337 H340
• 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:1o1t, PDBe:1o1t, PDBj:1o1t
• PDBsum: 1o1t
• PubMed: 12667062
• UniProt: Q02293|FNTB_RAT Protein farnesyltransferase subunit beta (Gene Name=Fntb)