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1JCS

CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH THE PEPTIDE SUBSTRATE TKCVFM AND AN ANALOG OF FARNESYL DIPHOSPHATE

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
CCYS3

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FII B 1002
ChainResidue
BCYS254
BARG291
BLYS294
BTYR300
BTRP303
BTYR361
BHOH1162
BHOH1164
BHOH1165
BHOH1168
BHOH1198
CVAL4
CPHE5
CHOH1253
ATYR166
ATYR200
BTYR205
BHIS248
BGLY250

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 3002
ChainResidue
BLEU89
BTHR90
BTYR93
BHOH1183
BACY3003

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY B 3003
ChainResidue
BTYR81
BTYR93
BARG358
BASP359
BACY3002

site_idAC5
Number of Residues24
DetailsBINDING SITE FOR CHAIN C OF SYNTHETIC HEXAPEPTIDE TKCVFM
ChainResidue
ALYS164
ATYR166
AGLN167
AHOH1167
AHOH1310
BALA98
BSER99
BTRP102
BTRP106
BARG202
BASP297
BLYS356
BTYR361
BHIS362
BZN1001
BFII1002
BHOH1163
CHOH1184
CHOH1246
CHOH1253
CHOH1317
CHOH1318
CHOH1412
CHOH1568

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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