Brand  (β version)

PDB ID: 1JCQ

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Ligands
Code Name Style Show Link
739 2(S)-{2(S)-[2(R)-amino-3-mercapto]propylamino-3(S)-methyl}pentyloxy-3-phenylpropionylmethionine sulfone PoSSuM
ACY Acetic acid PoSSuM
FPP Farnesyl diphosphate PoSSuM
ZN Zinc ion PoSSuM
FRU Beta-D-fructofuranose PoSSuM
GLC Alpha-D-glucopyranose PoSSuM
: Polysaccharide
Non-standard Residues
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Structure summary

Code : 1JCQ   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : CRYSTAL STRUCTURE OF HUMAN PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH FARNESYL DIPHOSPHATE AND THE PEPTIDOMIMETIC INHIBITOR L-739,750
Release Data : 2001-11-02
Compound :
mol_id molecule chains synonym
1 PROTEIN FARNESYLTRANSFERASE, ALPHA SUBUNIT A CAAX FARNESYLTRANSFERASE ALPHA SUBUNIT; RAS PROTEINS PRENYLTRANSFERASE ALPHA; FTASE-ALPHA; PRENYL-PROTEIN TRANSFERASE RAM2 HOMOLOG
ec: 2.5.1.-
fragment: ALPHA SUBUNIT
mutation: GLU-GLU-PHE TAG ON THE C-TERMINUS
mol_id molecule chains synonym
2 PROTEIN FARNESYLTRANSFERASE, BETA SUBUNIT B CAAX FARNESYLTRANSFERASE BETA SUBUNIT; RAS PROTEINS PRENYLTRANSFERASE BETA; FTASE-BETA; PRENYL-PROTEIN TRANSFERASE DPR1/RAM1 SUBUNIT
ec: 2.5.1.-
fragment: BETA SUBUNIT
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
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, TUMOR REGRESSION, L-739, 750, PEPTIDOMIMETIC, INHIBITOR, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.30 Å )
Citation :

The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics.

Long, S.B.,Hancock, P.J.,Kral, A.M.  et al.
(2001)  Proc.Natl.Acad.Sci.USA  98 : 12948 - 12953

PubMed: 11687658
DOI: 10.1073/pnas.241407898

The Basis for K-Ras4B Binding Specificity to Protein Farnesyltransferase Revealed by 2A 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 2.25A Resolution

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

DOI: 10.1126/science.275.5307.1800

Reaction

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
-
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
-