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1D8D

CO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE SUBSTRATE AND FPP ANALOG AT 2.0A RESOLUTION

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
A0007323biological_processpeptide pheromone maturation
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 Residues9
DetailsBINDING SITE FOR RESIDUE ACT P 3000
ChainResidue
BTYR93
BCYS95
BLEU96
BASP359
PLYS3
PLYS7
PHOH1166
PHOH1330
PACT3001

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT P 3001
ChainResidue
BLEU96
BTYR361
PLYS3
PCYS8
PHOH1246
PHOH1318
PACT3000

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 3002
ChainResidue
BLEU89
BTHR90
BTYR93
BHOH1183
BHOH1449
BACT3003

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 3003
ChainResidue
BTYR81
BTYR93
BARG358
BASP359
BHOH1449
BACT3002

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
BASP297
BCYS299
BHIS362
PCYS8

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FII B 1000
ChainResidue
ALYS164
ATYR166
BHIS248
BGLY250
BCYS254
BARG291
BLYS294
BTYR300
BTRP303
BHOH1162
BHOH1164
BHOH1165
BHOH1168
BHOH1198
BHOH1253
PILE10

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000269|PubMed:27791178, ECO:0007744|PDB:5TAR, ECO:0007744|PDB:5TB5
ChainResidueDetails
PCYS8
BARG291
BTYR300

site_idSWS_FT_FI2
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000305|PubMed:29239724
ChainResidueDetails
PLYS3
BCYS299
BHIS362

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: N6-palmitoyl lysine => ECO:0000269|PubMed:29239724
ChainResidueDetails
PLYS5

site_idSWS_FT_FI4
Number of Residues1
DetailsLIPID: N6-palmitoyl lysine => ECO:0000305|PubMed:29239724
ChainResidueDetails
PLYS7

site_idSWS_FT_FI5
Number of Residues1
DetailsLIPID: S-farnesyl cysteine => ECO:0000269|PubMed:27791178, ECO:0000305|PubMed:24415755, ECO:0007744|PDB:5TAR, ECO:0007744|PDB:5TB5
ChainResidueDetails
PCYS8

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 2024-11-06

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