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1FT2

CO-CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A FARNESYL DIPHOSPHATE SUBSTRATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0008318molecular_functionprotein prenyltransferase activity
A0018342biological_processprotein prenylation
B0003824molecular_functioncatalytic activity
B0004311molecular_functionfarnesyltranstransferase activity
B0004659molecular_functionprenyltransferase activity
B0004660molecular_functionprotein farnesyltransferase activity
B0005515molecular_functionprotein binding
B0005875cellular_componentmicrotubule associated complex
B0005965cellular_componentprotein farnesyltransferase complex
B0006629biological_processlipid metabolic process
B0008270molecular_functionzinc ion binding
B0008283biological_processcell population proliferation
B0008284biological_processpositive regulation of cell population proliferation
B0008285biological_processnegative regulation of cell population proliferation
B0008318molecular_functionprotein prenyltransferase activity
B0010035biological_processresponse to inorganic substance
B0014070biological_processresponse to organic cyclic compound
B0016740molecular_functiontransferase activity
B0018343biological_processprotein farnesylation
B0034097biological_processresponse to cytokine
B0042060biological_processwound healing
B0042277molecular_functionpeptide binding
B0045787biological_processpositive regulation of cell cycle
B0046872molecular_functionmetal ion binding
B0048144biological_processfibroblast proliferation
B0048145biological_processregulation of fibroblast proliferation
B0048146biological_processpositive regulation of fibroblast proliferation
B0051770biological_processpositive regulation of nitric-oxide synthase biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1001
ChainResidue
BASP297
BCYS299
BTYR361
BHIS362

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FPP B 1
ChainResidue
BLYS294
BTYR300
ALYS164
BHIS248
BGLY250
BCYS254
BARG291

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING:
ChainResidueDetails
BTYR300
BHIS248
BARG291

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18844669, ECO:0000269|PubMed:20056542, ECO:0000269|PubMed:9065406
ChainResidueDetails
BCYS299
BHIS362
BASP297

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important for selectivity against geranylgeranyl diphosphate => ECO:0000250|UniProtKB:P49356
ChainResidueDetails
BTRP102

Catalytic Information from CSA
site_idMCSA1
Number of Residues9
DetailsM-CSA 484
ChainResidueDetails
BHIS248electrostatic stabiliser
BARG291electrostatic stabiliser
BLYS294electrostatic stabiliser
BASP297metal ligand
BCYS299metal ligand
BTYR300electrostatic stabiliser
BASP352metal ligand
BASP359electrostatic stabiliser
BHIS362metal ligand

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PDB entries from 2024-04-17

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