Structure of PDB 1jcs Chain A Binding Site BS02

Receptor Information

>1jcs Chain A (length=323) Species: 10116 (Rattus norvegicus)

FLSLDSPTYVLYRDRAEWADIDPVPQNDGPSPVVQIIYSEKFRDVYDYFR
AVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLRSLQKDLQEEMNY
IIAIIEEQPKNYQVWHHRRVLVEWLKDPSQELEFIADILNQDAKNYHAWQ
HRQWVIQEFRLWDNELQYVDQLLKEDVRNNSVWNQRHFVISNTTGYSDRA
VLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSRYPNLLNQLLDLQP
SHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKE
YWRYIGRSLQSKHSRESDIPASV

Ligand information

• Ligand ID: FII
• InChI: InChI=1S/C17H30NO5P/c1-14(2)7-5-8-15(3)9-6-10-16(4)11-12-23-18-17(19)13-24(20,21)22/h7,9,11H,5-6,8,10,12-13H2,1-4H3,(H,18,19)(H2,20,21,22)/b15-9+,16-11+
• InChIKey: JAOBYUCYSAOLHS-XGGJEREUSA-N
• SMILES:
  ACDLabs 10.04: O=C(NOC\C=C(/C)CC\C=C(/C)CC\C=C(/C)C)CP(=O)(O)O
  OpenEye OEToolkits 1.5.0: CC(=CCCC(=CCCC(=CCONC(=O)CP(=O)(O)O)C)C)C
  OpenEye OEToolkits 1.5.0: CC(=CCC/C(=C/CC/C(=C/CONC(=O)CP(=O)(O)O)/C)/C)C
  CACTVS 3.341: CC(C)=CCC\C(C)=C\CC\C(C)=C\CONC(=O)C[P](O)(O)=O
  CACTVS 3.341: CC(C)=CCCC(C)=CCCC(C)=CCONC(=O)C[P](O)(O)=O
• Formula: C17 H30 N O5 P
• Name: [(3,7,11-TRIMETHYL-DODECA-2,6,10-TRIENYLOXYCARBAMOYL)-METHYL]-PHOSPHONIC ACID;
  FPP ANALOG
• DrugBank: DB07771
• ZINC: ZINC000002046984
• PDB chain: 1jcs Chain B Residue 1002

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1jcs The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics.
• Resolution: 2.2 Å
• Binding residue (original residue number in PDB): Y166 Y200
• Binding residue (residue number reindexed from 1): Y112 Y146
• Annotation score: 2

Enzymatic activity

• Catalytic site (original residue number in PDB): K164
• Catalytic site (residue number reindexed from 1): K110
• Enzyme Commision number: 2.5.1.58: protein farnesyltransferase.
  2.5.1.59: protein geranylgeranyltransferase type I.

Gene Ontology

Molecular Function

• GO:0004659 prenyltransferase activity
• GO:0004660 protein farnesyltransferase activity
• GO:0004661 protein geranylgeranyltransferase activity
• GO:0004662 CAAX-protein geranylgeranyltransferase activity
• GO:0004663 Rab geranylgeranyltransferase activity
• GO:0005515 protein binding
• GO:0008017 microtubule binding
• GO:0008270 zinc ion binding
• GO:0008318 protein prenyltransferase activity
• GO:0030971 receptor tyrosine kinase binding
• GO:0036094 small molecule binding
• GO:0042277 peptide binding
• GO:0043014 alpha-tubulin binding
• GO:0060090 molecular adaptor activity
• GO:1901363 heterocyclic compound binding

Biological Process

• GO:0007167 enzyme-linked receptor protein signaling pathway
• GO:0008284 positive regulation of cell population proliferation
• GO:0014070 response to organic cyclic compound
• GO:0018342 protein prenylation
• GO:0018343 protein farnesylation
• GO:0018344 protein geranylgeranylation
• GO:0034097 response to cytokine
• GO:0035022 positive regulation of Rac protein signal transduction
• GO:0043066 negative regulation of apoptotic process
• GO:0045787 positive regulation of cell cycle
• GO:0051770 positive regulation of nitric-oxide synthase biosynthetic process
• GO:0051771 negative regulation of nitric-oxide synthase biosynthetic process
• GO:0090044 positive regulation of tubulin deacetylation
• GO:1904395 positive regulation of skeletal muscle acetylcholine-gated channel clustering

Cellular Component

• GO:0005737 cytoplasm
• GO:0005875 microtubule associated complex
• GO:0005953 CAAX-protein geranylgeranyltransferase complex
• GO:0005965 protein farnesyltransferase complex

External links

• PDB: RCSB:1jcs, PDBe:1jcs, PDBj:1jcs
• PDBsum: 1jcs
• PubMed: 11687658
• UniProt: Q04631|FNTA_RAT Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (Gene Name=Fnta)