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

2F0Y

Crystal Structure Of Human Protein Farnesyltransferase Complexed With Farnesyl Diphosphate and hydantoin derivative

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
A0007167biological_processenzyme-linked receptor protein signaling pathway
A0007179biological_processtransforming growth factor beta receptor signaling pathway
A0007528biological_processneuromuscular junction development
A0008017molecular_functionmicrotubule binding
A0008318molecular_functionprotein prenyltransferase activity
A0018342biological_processprotein prenylation
A0018343biological_processprotein farnesylation
A0018344biological_processprotein geranylgeranylation
A0030971molecular_functionreceptor tyrosine kinase binding
A0035022biological_processpositive regulation of Rac protein signal transduction
A0043014molecular_functionalpha-tubulin binding
A0060090molecular_functionmolecular adaptor activity
A0071340biological_processskeletal muscle acetylcholine-gated channel clustering
A0090044biological_processpositive regulation of tubulin deacetylation
A0090045biological_processpositive regulation of deacetylase activity
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
B0008318molecular_functionprotein prenyltransferase activity
B0018343biological_processprotein farnesylation
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BASP297
BCYS299
BHIS362
B3MN963

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FPP B 1001
ChainResidue
BGLY250
BTYR251
BCYS254
BARG291
BLYS294
BTYR300
BTRP303
B3MN963
BHOH1011
BHOH1014
BHOH1024
BHOH1142
BHOH1186
ALYS164
ATYR166
AHIS201
BARG202
BHIS248

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 3MN B 963
ChainResidue
BTYR93
BLEU96
BSER99
BTRP102
BASP297
BTYR300
BASP359
BPHE360
BTYR361
BZN501
BFPP1001

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11687658, ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:16893176
ChainResidueDetails
BHIS248
BARG291
BTYR300

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11687658, ECO:0000269|PubMed:12036349, ECO:0000269|PubMed:12825937, ECO:0000269|PubMed:15451670, ECO:0000269|PubMed:16893176, ECO:0000269|PubMed:19246009
ChainResidueDetails
BASP297
BCYS299
BHIS362

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important for selectivity against geranylgeranyl diphosphate => ECO:0000269|PubMed:16893176
ChainResidueDetails
BTRP102

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q8K2I1
ChainResidueDetails
BTHR436

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon