Brand  (β version)

PDB ID: 1D8D

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Ligands
Code Name Style Show Link
ACT Acetate ion PoSSuM
FII [(3,7,11-trimethyl-dodeca-2,6,10-trienyloxycarbamoyl)-methyl]-phosphonic acid PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
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Structure summary

Code : 1D8D   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : CO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE SUBSTRATE AND FPP ANALOG AT 2.0A RESOLUTION
Release Data : 2000-02-09
Compound :
mol_id molecule chains synonym
1 farnesyltransferase (alpha subunit) A FTASE
ec: 2.5.1.21
fragment: alpha subunit
mol_id molecule chains synonym
2 farnesyltransferase (beta subunit) B FTASE
ec: 2.5.1.21
fragment: beta subunit
mol_id molecule chains
3 K-RAS4B PEPTIDE SUBSTRATE P
Source :
mol_id organism_scientific organism_common expression_system
1 Rattus norvegicus  (taxid:10116) Norway rat Spodoptera frugiperda  (taxid:7108)
organ: BRAIN
expression_system_common: Fall armyworm
expression_system_atcc_number: 63134
mol_id organism_scientific organism_common expression_system
2 Rattus norvegicus  (taxid:10116) Norway rat Spodoptera frugiperda  (taxid:7108)
organ: BRAIN
expression_system_common: Fall armyworm
expression_system_atcc_number: 63134
mol_id organism_scientific
3
synthetic: yes
other_details: This synthetic peptide is derived from human K-Ras4B, residues 178-188.
Authors : Long, S.B., Casey, P.J., Beese, L.S.
Keywords : FTASE, PFT, PFTASE, FARNESYLTRANSFERASE, FARNESYL TRANSFERASE, CAAX, RAS, CANCER, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.00 Å )
Citation :

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 Fold.Des.  8 : 209 - 222

PubMed: 10673434
DOI: 10.1016/S0969-2126(00)00096-4

Crystal Structure of Protein Farnesyltransferase at 2.25A 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 Mammalian Protein Farnesyltransferase 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:
(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein] 2.5.1.58 PubMed:12657282, PubMed:18844669, PubMed:19219049, PubMed:22963166
-
geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein] 2.5.1.59 PubMed:14609943, PubMed:19219049
-
Chain : B
UniProt : Q02293 (FNTB_RAT)
Reaction: EC: Evidence:
Physiological Direction:
(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein] 2.5.1.58 PubMed:10673434, PubMed:18844669, PubMed:19219049, PubMed:19246009, PubMed:22963166
-
Chain : P
UniProt : P01116 (RASK_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
GTP + H2O = GDP + H(+) + phosphate 3.6.5.2 PubMed:20949621
-