Brand  (β version)

PDB ID: 1KZP

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Ligands
Code Name Style Show Link
ACY Acetic acid PoSSuM
FAR Farnesyl PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 1KZP   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE/TRANSFERASE SUBSTRATE
Title : PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A FARNESYLATED K-RAS4B PEPTIDE PRODUCT
Release Data : 2002-10-16
Compound :
mol_id molecule chains synonym
1 Protein Farnesyltransferase alpha subunit A CAAX FARNESYLTRANSFERASE ALPHA SUBUNIT, RAS PROTEINS PRENYLTRANSFERASE ALPHA, FTASE-ALPHA
ec: 2.5.1.21
mol_id molecule chains synonym
2 Protein Farnesyltransferase beta subunit B CAAX FARNESYLTRANSFERASE BETA SUBUNIT, RAS PROTEINS PRENYLTRANSFERASE BETA, FTASE-BETA
ec: 2.5.1.21
mol_id molecule chains synonym
3 Farnesylated K-Ras4B peptide product C TRANSFORMING PROTEIN P21B
Source :
mol_id organism_scientific organism_common expression_system
1 Rattus norvegicus  (taxid:10116) Norway rat Spodoptera frugiperda  (taxid:7108)
expression_system_common: Fall armyworm
expression_system_atcc_number: 63134
expression_system_vector_type: baculovirus
mol_id organism_scientific organism_common expression_system
2 Rattus norvegicus  (taxid:10116) Norway rat Spodoptera frugiperda  (taxid:7108)
expression_system_common: Fall armyworm
expression_system_atcc_number: 63134
expression_system_vector_type: baculovirus
mol_id organism_scientific
3
synthetic: yes
other_details: THE PROTEIN WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE OF THE PROTEIN IS NATURALLY FOUND IN HOMO SAPIENS.
Authors : Long, S.B., Casey, P.J., Beese, L.S.
Keywords : FTASE, PFT, PFTASE, FT, FPT, FARNESYLTRANSFERASE, FARNESYL TRANSFERASE, FARNESYL PROTEIN TRANSFERASE, CAAX, RAS CANCER, TRANSFERASE-TRANSFERASE SUBSTRATE COMPLEX
Exp. method : X-RAY DIFFRACTION ( 2.10 Å )
Citation :

Reaction path of protein farnesyltransferase at atomic resolution

Long, S.B.,Casey, P.J.,Beese, L.S.
(2002)  Nature  419 : 645 - 650

PubMed: 12374986
DOI: 10.1038/nature00986

The Basis for K-Ras4B Binding Specificity to Protein Farnesyltransferase Revealed by 2 A Resolution Ternary Complex Structures

Long, S.B.,Casey, P.J.,Beese, L.S.
(2000)  Structure  8 : 209 - 222

DOI: 10.1016/S0969-2126(00)00096-4

Crystal Structure of Protein Farnesyltransferase at 2.25 A Resolution

Park, H.W.,Boduluri, S.R.,Moomaw, J.F.  et al.
(1997)  Science  275 : 1800 - 1804

DOI: 10.1126/science.275.5307.1800

Co-Crystal Structure of Protein Farnesyltransferase Complexed with a Farnesyl Diphosphate Substrate

Long, S.B.,Casey, P.J.,Beese, L.S.
(1998)  Biochemistry  37 : 9612 - 9618

DOI: 10.1021/bi980708e

Reaction

Chain : A
UniProt : Q04631 (FNTA_RAT)
Reaction: EC: Evidence:
Physiological Direction:
L-cysteinyl-[protein] + (2E,6E)-farnesyl diphosphate = S- (2E,6E)-farnesyl-L-cysteinyl-[protein] + diphosphate 2.5.1.58 PubMed:12657282, PubMed:18844669, PubMed:19219049, PubMed:22963166
-
geranylgeranyl diphosphate + L-cysteinyl-[protein] = S- geranylgeranyl-L-cysteinyl-[protein] + diphosphate 2.5.1.59 PubMed:14609943, PubMed:19219049
-
Cofactor: Evidence: Note:
Mg(2+) ECO:0000250 | UniProtKB:P29703
-
Chain : B
UniProt : Q02293 (FNTB_RAT)
Reaction: EC: Evidence:
Physiological Direction:
L-cysteinyl-[protein] + (2E,6E)-farnesyl diphosphate = S- (2E,6E)-farnesyl-L-cysteinyl-[protein] + diphosphate 2.5.1.58 PubMed:10673434, PubMed:18844669, PubMed:19219049, PubMed:19246009, PubMed:22963166
-
Cofactor: Evidence: Note:
Zn(2+) ECO:0000269 | PubMed:10673434
ECO:0000269 | PubMed:12374986
ECO:0000269 | PubMed:12667062
ECO:0000269 | PubMed:15451670
ECO:0000269 | PubMed:18844669
ECO:0000269 | PubMed:19219049
ECO:0000269 | PubMed:19246009
ECO:0000269 | PubMed:20056542
ECO:0000269 | PubMed:22963166
ECO:0000269 | PubMed:9609683
ECO:0000269 | PubMed:9657673
ECO:0000269 | PubMed:9843427
Binds 1 zinc ion per subunit.
Chain : C
UniProt : P01118 (RASK_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
GTP + H2O = GDP + phosphate + H(+) 3.6.5.2 PubMed:20949621, PubMed:39809765
-