Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1O1R

Structure of FPT bound to GGPP

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
A0014070biological_processresponse to organic cyclic compound
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
B0014070biological_processresponse to organic cyclic compound
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
BHOH2375

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GRG B 2001
ChainResidue
BHIS248
BGLY250
BTYR251
BCYS254
BARG291
BLYS294
BTYR300
BTRP303
BHOH2009
BHOH2373
BHOH2374
BHOH2380
BHOH2381
ALYS164
ATYR166
ATYR200
AHIS201
BTYR205

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

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

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon