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1O5M

Structure of FPT bound to the inhibitor SCH66336

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
A0005875cellular_componentmicrotubule associated complex
A0005953cellular_componentCAAX-protein geranylgeranyltransferase complex
A0005965cellular_componentprotein farnesyltransferase complex
A0007167biological_processenzyme-linked receptor protein signaling pathway
A0008017molecular_functionmicrotubule binding
A0008270molecular_functionzinc ion binding
A0008284biological_processpositive regulation of cell population proliferation
A0008318molecular_functionprotein prenyltransferase activity
A0010035biological_processresponse to inorganic substance
A0014070biological_processresponse to organic cyclic compound
A0016740molecular_functiontransferase activity
A0018342biological_processprotein prenylation
A0018343biological_processprotein farnesylation
A0018344biological_processprotein geranylgeranylation
A0030971molecular_functionreceptor tyrosine kinase binding
A0034097biological_processresponse to cytokine
A0035022biological_processpositive regulation of Rac protein signal transduction
A0036094molecular_functionsmall molecule binding
A0042277molecular_functionpeptide binding
A0043014molecular_functionalpha-tubulin binding
A0043066biological_processnegative regulation of apoptotic process
A0045787biological_processpositive regulation of cell cycle
A0051770biological_processpositive regulation of nitric-oxide synthase biosynthetic process
A0051771biological_processnegative regulation of nitric-oxide synthase biosynthetic process
A0060090molecular_functionmolecular adaptor activity
A0090044biological_processpositive regulation of tubulin deacetylation
A1901363molecular_functionheterocyclic compound binding
A1904395biological_processpositive regulation of skeletal muscle acetylcholine-gated channel clustering
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
BHIS362
BHOH3388

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FPP B 2001
ChainResidue
BTYR205
BHIS248
BGLY250
BARG291
BLYS294
BTYR300
BTRP303
BHOH3009
BHOH3031
BHOH3105
BHOH3387
ALYS164
ATYR166
AHOH383
AHOH384
BTRP102

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 336 B 3001
ChainResidue
ALYS164
ATYR166
AHIS201
BALA92
BCYS95
BLEU96
BSER99
BTRP102
BTRP106
BASP359
BTYR361
BHOH3275
BHOH3385

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

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

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

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8K2I1
ChainResidueDetails
BSER432

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q8K2I1
ChainResidueDetails
BTHR436

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 2024-04-24

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