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Chlorine in PDB 2zir: Crystal Structure of Rat Protein Farnesyltransferase Complexed with A Benzofuran Inhibitor and Fpp

Enzymatic activity of Crystal Structure of Rat Protein Farnesyltransferase Complexed with A Benzofuran Inhibitor and Fpp

All present enzymatic activity of Crystal Structure of Rat Protein Farnesyltransferase Complexed with A Benzofuran Inhibitor and Fpp:
2.5.1.58;

Protein crystallography data

The structure of Crystal Structure of Rat Protein Farnesyltransferase Complexed with A Benzofuran Inhibitor and Fpp, PDB code: 2zir was solved by T.A.Fukami, S.Sogabe, Y.Nagata, O.Kondoh, N.Ishii, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.00 / 2.40
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 171.996, 171.996, 69.179, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 2zir:

The structure of Crystal Structure of Rat Protein Farnesyltransferase Complexed with A Benzofuran Inhibitor and Fpp also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Rat Protein Farnesyltransferase Complexed with A Benzofuran Inhibitor and Fpp (pdb code 2zir). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Rat Protein Farnesyltransferase Complexed with A Benzofuran Inhibitor and Fpp, PDB code: 2zir:

Chlorine binding site 1 out of 1 in 2zir

Go back to Chlorine Binding Sites List in 2zir
Chlorine binding site 1 out of 1 in the Crystal Structure of Rat Protein Farnesyltransferase Complexed with A Benzofuran Inhibitor and Fpp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Rat Protein Farnesyltransferase Complexed with A Benzofuran Inhibitor and Fpp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl903

b:43.1
occ:1.00
 CL27 B:NH7903 0.0 43.1 1.0
C24 B:NH7903 1.7 42.5 1.0
C23 B:NH7903 2.7 42.4 1.0
C25 B:NH7903 2.7 42.1 1.0
O B:HOH1164 3.2 53.9 1.0
C7 B:FPP902 3.7 35.4 1.0
OH A:TYR166 3.8 34.0 1.0
C11 B:FPP902 3.9 31.0 1.0
C8 B:FPP902 3.9 33.7 1.0
CD B:ARG202 3.9 29.5 1.0
C22 B:NH7903 4.0 42.3 1.0
C26 B:NH7903 4.0 42.4 1.0
CE1 A:TYR166 4.0 33.9 1.0
C9 B:FPP902 4.1 32.5 1.0
C15 B:FPP902 4.1 30.0 1.0
NH1 B:ARG202 4.2 30.6 1.0
C5 B:FPP902 4.3 37.9 1.0
CZ A:TYR166 4.3 34.0 1.0
O3 B:GOL925 4.4 61.9 1.0
O B:HOH1089 4.4 51.0 1.0
C6 B:FPP902 4.5 36.9 1.0
C21 B:NH7903 4.5 42.5 1.0
C35 B:NH7903 4.6 44.2 1.0
NE B:ARG202 4.6 29.8 1.0
C3 B:GOL925 4.7 61.6 1.0
C10 B:FPP902 4.7 32.8 1.0
CZ B:ARG202 4.8 30.7 1.0
C12 B:FPP902 4.9 29.9 1.0
C13 B:FPP902 5.0 30.0 1.0
CG B:ARG202 5.0 29.4 1.0

Reference:

K.Asoh, M.Kohchi, I.Hyoudoh, T.Ohtsuka, M.Masubuchi, K.Kawasaki, H.Ebiike, Y.Shiratori, T.A.Fukami, O.Kondoh, T.Tsukaguchi, N.Ishii, Y.Aoki, N.Shimma, M.Sakaitani. Synthesis and Structure-Activity Relationships of Novel Benzofuran Farnesyltransferase Inhibitors Bioorg.Med.Chem.Lett. V. 19 1753 2009.
ISSN: ISSN 0960-894X
PubMed: 19217288
DOI: 10.1016/J.BMCL.2009.01.074
Page generated: Sat Dec 12 09:30:30 2020

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