Atomistry » Zinc » PDB 2zep-2zxg » 2zir
Atomistry »
  Zinc »
    PDB 2zep-2zxg »
      2zir »

Zinc 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:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Rat Protein Farnesyltransferase Complexed with A Benzofuran Inhibitor and Fpp, PDB code: 2zir:

Zinc binding site 1 out of 1 in 2zir

Go back to Zinc Binding Sites List in 2zir
Zinc 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 Zinc with other atoms in the Zn 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:Zn901

b:30.3
occ:1.00
 OD1 B:ASP297 2.0 25.2 1.0
N3 B:NH7903 2.0 42.5 1.0
SG B:CYS299 2.3 28.6 1.0
NE2 B:HIS362 2.3 35.2 1.0
OD2 B:ASP297 2.5 27.1 1.0
CG B:ASP297 2.5 26.6 1.0
C2 B:NH7903 2.9 42.1 1.0
C4 B:NH7903 3.0 42.0 1.0
CD2 B:HIS362 3.2 34.5 1.0
CE1 B:HIS362 3.3 35.2 1.0
CB B:CYS299 3.3 26.5 1.0
CE2 B:TYR361 3.8 30.3 1.0
CB B:ASP297 4.0 26.4 1.0
N B:CYS299 4.0 27.3 1.0
N1 B:NH7903 4.1 42.3 1.0
C5 B:NH7903 4.1 42.5 1.0
CA B:CYS299 4.2 27.4 1.0
CG B:HIS362 4.3 34.5 1.0
ND1 B:HIS362 4.3 35.7 1.0
O B:HOH1010 4.4 27.9 1.0
OD2 B:ASP352 4.5 40.5 1.0
OH B:TYR361 4.5 31.1 1.0
CG B:ASP352 4.6 39.2 1.0
CZ B:TYR361 4.6 30.1 1.0
CD2 B:TYR361 4.7 29.6 1.0
CB B:ASP352 4.7 39.0 1.0
O B:HOH1160 4.9 50.4 1.0
CA B:ASP352 4.9 39.0 1.0
C B:ASP297 4.9 28.4 1.0
CA B:ASP297 5.0 27.8 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: Thu Oct 24 10:47:36 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy