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1KZO

PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYLATED K-RAS4B PEPTIDE PRODUCT AND FARNESYL DIPHOSPHATE SUBSTRATE BOUND SIMULTANEOUSLY

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
A0010698molecular_functionacetyltransferase activator activity
A0016740molecular_functiontransferase activity
A0018342biological_processprotein prenylation
A0018343biological_processprotein farnesylation
A0018344biological_processprotein geranylgeranylation
A0019899molecular_functionenzyme binding
A0030971molecular_functionreceptor tyrosine kinase binding
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
A0060090molecular_functionmolecular adaptor activity
A0060632biological_processregulation of microtubule-based movement
A0080120biological_processCAAX-box protein maturation
A1901363molecular_functionheterocyclic compound binding
B0003824molecular_functioncatalytic activity
B0004311molecular_functiongeranylgeranyl diphosphate synthase 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
B0008284biological_processpositive regulation of cell population proliferation
B0008285biological_processnegative regulation of cell population proliferation
B0008318molecular_functionprotein prenyltransferase activity
B0010698molecular_functionacetyltransferase activator activity
B0016740molecular_functiontransferase activity
B0018343biological_processprotein farnesylation
B0019899molecular_functionenzyme binding
B0042060biological_processwound healing
B0042277molecular_functionpeptide binding
B0045787biological_processpositive regulation of cell cycle
B0046872molecular_functionmetal ion binding
B0048145biological_processregulation of fibroblast proliferation
B0048146biological_processpositive regulation of fibroblast proliferation
B0060632biological_processregulation of microtubule-based movement
B0080120biological_processCAAX-box protein maturation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1001
ChainResidue
BASP297
BCYS299
BHIS362
BHOH3212

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FAR C 12
ChainResidue
CCYS8
BALA92
BSER357
BASP359
BTYR361
CLYS7

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE FPP B 1002
ChainResidue
ALYS164
ATYR166
AHOH1245
BHIS248
BGLY250
BCYS254
BARG291
BLYS294
BTYR300
BTRP303
BHOH3070
BHOH3071
BHOH3164
BHOH3176
BHOH3196
CVAL9
CILE10

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACY B 3002
ChainResidue
BLEU89
BTHR90
BTYR93
BHOH3075

site_idAC5
Number of Residues25
DetailsBINDING SITE FOR CHAIN C OF FARNESYLATED K-RAS4B PEPTIDE PRODUCT
ChainResidue
ATYR166
AGLN167
AHOH1167
AHOH1310
AHOH1655
BCYS95
BALA98
BSER99
BTRP102
BTRP106
BALA151
BARG202
BTYR361
BFPP1002
BHOH3197
BHOH3198
CFAR12
CHOH1163
CHOH1184
CHOH1313
CHOH1618
CHOH1644
CHOH1665
CHOH1681
CHOH1686

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsRepeat: {"description":"PFTA 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues34
DetailsRepeat: {"description":"PFTA 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues32
DetailsRepeat: {"description":"PFTA 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues34
DetailsRepeat: {"description":"PFTA 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues34
DetailsRepeat: {"description":"PFTA 5"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues41
DetailsRepeat: {"description":"PFTB 1"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues41
DetailsRepeat: {"description":"PFTB 2"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues41
DetailsRepeat: {"description":"PFTB 3"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues42
DetailsRepeat: {"description":"PFTB 4"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues42
DetailsRepeat: {"description":"PFTB 5"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18844669","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20056542","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9065406","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsSite: {"description":"Important for selectivity against geranylgeranyl diphosphate","evidences":[{"source":"UniProtKB","id":"P49356","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsPropeptide: {"description":"Removed in mature form","featureId":"PRO_0000281291","evidences":[{"source":"PubMed","id":"27791178","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Cysteine methyl ester","evidences":[{"source":"PubMed","id":"27791178","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TAR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TB5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsLipidation: {"description":"N6-palmitoyl lysine","evidences":[{"source":"PubMed","id":"29239724","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues1
DetailsLipidation: {"description":"S-farnesyl cysteine","evidences":[{"source":"PubMed","id":"27791178","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24415755","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5TAR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TB5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

246704

PDB entries from 2025-12-24

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