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Ligands
Code Name Style Show Link
ACY Acetic acid
FII [(3,7,11-trimethyl-dodeca-2,6,10-trienyloxycarbamoyl)-methyl]-phosphonic acid
ZN Zinc ion
FRU Beta-D-fructofuranose
GLC Alpha-D-glucopyranose
: Polysaccharide
Non-standard Residues
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Code : 1TN6   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Protein Farnesyltransferase Complexed with a Rap2a Peptide Substrate and a FPP Analog at 1.8A Resolution
Release Data : 2004-11-02
Compound :
mol_id molecule chains synonym
1 Protein farnesyltransferase alpha subunit A CAAX farnesyltransferase alpha subunit, FTase-alpha
ec: 2.5.1.58
mutation: Insertion: Glu A380, Glu A381, Phe A382
mol_id molecule chains synonym
2 Protein farnesyltransferase beta subunit B CAAX farnesyltransferase beta subunit, FTase-beta
ec: 2.5.1.58
mol_id molecule chains
3 peptide derived from the C-terminus of Rap2a C
fragment: Rap2a C-terminal peptide
mutation: C176T, C177A
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli BL21(DE3)  (taxid:469008)
gene: FNTA
expression_system_strain: BL21-DE3
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Escherichia coli BL21(DE3)  (taxid:469008)
gene: FNTB
expression_system_strain: BL21-DE3
mol_id organism_scientific
3
synthetic: yes
other_details: peptide was chemically synthesized. The sequence of this pepetide naturally occurs in Homo sapiens
Authors : Reid, T.S., Terry, K.L., Casey, P.J., Beese, L.S.
Keywords : FTase, farnesyltransferase, farnesyl transferase, prenyltransferase, CaaX, Ras, lipid modification, prenylation, substrate selectivity, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 1.80 Å )
Citation :

Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity

Reid, T.S.,Terry, K.L.,Casey, P.J.  et al.
(2004)  J.Mol.Biol.  343 : 417 - 433

PubMed: 15451670
DOI: 10.1016/j.jmb.2004.08.056

Chain : A
UniProt : P49354 (FNTA_HUMAN)
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:12036349, PubMed:12825937, PubMed:16893176, PubMed:19246009, PubMed:8419339, PubMed:8494894
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geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein] 2.5.1.59 PubMed:16893176
-
Chain : B
UniProt : P49356 (FNTB_HUMAN)
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:12036349, PubMed:12825937, PubMed:16893176, PubMed:19246009, PubMed:8494894
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