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1JCQ

CRYSTAL STRUCTURE OF HUMAN PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYL DIPHOSPHATE AND THE PEPTIDOMIMETIC INHIBITOR L-739,750

Functional Information from GO Data
ChainGOidnamespacecontents
A0004659molecular_functionprenyltransferase activity
A0004660molecular_functionprotein farnesyltransferase activity
A0004661molecular_functionprotein geranylgeranyltransferase activity
A0004662molecular_functionCAAX-protein geranylgeranyltransferase activity
A0004663molecular_functionRab geranylgeranyltransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005875cellular_componentmicrotubule associated complex
A0005886cellular_componentplasma membrane
A0005953cellular_componentCAAX-protein geranylgeranyltransferase complex
A0005965cellular_componentprotein farnesyltransferase complex
A0006998biological_processnuclear envelope organization
A0007167biological_processenzyme-linked receptor protein signaling pathway
A0007179biological_processtransforming growth factor beta receptor signaling pathway
A0007323biological_processpeptide pheromone maturation
A0007528biological_processneuromuscular junction development
A0008017molecular_functionmicrotubule binding
A0008318molecular_functionprotein prenyltransferase activity
A0010698molecular_functionacetyltransferase activator activity
A0016740molecular_functiontransferase activity
A0018342biological_processprotein prenylation
A0018343biological_processprotein farnesylation
A0018344biological_processprotein geranylgeranylation
A0019899molecular_functionenzyme binding
A0030971molecular_functionreceptor tyrosine kinase binding
A0035022biological_processpositive regulation of Rac protein signal transduction
A0043014molecular_functionalpha-tubulin binding
A0051604biological_processprotein maturation
A0060090molecular_functionmolecular adaptor activity
A0060632biological_processregulation of microtubule-based movement
A0071340biological_processskeletal muscle acetylcholine-gated channel clustering
A1904395biological_processpositive regulation of skeletal muscle acetylcholine-gated channel clustering
B0003824molecular_functioncatalytic activity
B0004659molecular_functionprenyltransferase activity
B0004660molecular_functionprotein farnesyltransferase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0005875cellular_componentmicrotubule associated complex
B0005965cellular_componentprotein farnesyltransferase complex
B0006629biological_processlipid metabolic process
B0008270molecular_functionzinc ion binding
B0008284biological_processpositive regulation of cell population proliferation
B0008318molecular_functionprotein prenyltransferase activity
B0010698molecular_functionacetyltransferase activator activity
B0016740molecular_functiontransferase activity
B0018343biological_processprotein farnesylation
B0019899molecular_functionenzyme binding
B0042277molecular_functionpeptide binding
B0045787biological_processpositive regulation of cell cycle
B0046872molecular_functionmetal ion binding
B0060632biological_processregulation of microtubule-based movement
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsRepeat: {"description":"PFTA 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues33
DetailsRepeat: {"description":"PFTA 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues34
DetailsRepeat: {"description":"PFTA 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues33
DetailsRepeat: {"description":"PFTA 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues34
DetailsRepeat: {"description":"PFTA 5"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues41
DetailsRepeat: {"description":"PFTB 1"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues41
DetailsRepeat: {"description":"PFTB 2"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues41
DetailsRepeat: {"description":"PFTB 3"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues42
DetailsRepeat: {"description":"PFTB 4"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues42
DetailsRepeat: {"description":"PFTB 5"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11687658","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12036349","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12825937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15451670","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16893176","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11687658","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12036349","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12825937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15451670","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16893176","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19246009","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsSite: {"description":"Important for selectivity against geranylgeranyl diphosphate","evidences":[{"source":"PubMed","id":"16893176","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d8d
ChainResidueDetails
ALYS164
BTYR300

238895

PDB entries from 2025-07-16

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