Atomistry » Zinc » PDB 2qyn-2rgl » 2r59
Atomistry »
  Zinc »
    PDB 2qyn-2rgl »
      2r59 »

Zinc in PDB 2r59: Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041

Enzymatic activity of Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041

All present enzymatic activity of Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041:
3.3.2.6;

Protein crystallography data

The structure of Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041, PDB code: 2r59 was solved by F.Tholander, J.Z.Haeggstrom, M.Thunnissen, A.Muroya, B.P.Roques, M.C.Fournie-Zaluski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.85 / 1.89
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.210, 87.230, 99.230, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 22.7

Other elements in 2r59:

The structure of Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041 also contains other interesting chemical elements:

Ytterbium (Yb) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041 (pdb code 2r59). 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 Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041, PDB code: 2r59:

Zinc binding site 1 out of 1 in 2r59

Go back to Zinc Binding Sites List in 2r59
Zinc binding site 1 out of 1 in the Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Leukotriene A4 Hydrolase Complexed with Inhibitor RB3041 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:16.9
occ:1.00
OE1 A:GLU318 1.9 18.2 1.0
O1 A:PH0706 1.9 18.3 1.0
NE2 A:HIS295 2.0 15.1 1.0
NE2 A:HIS299 2.0 17.9 1.0
CD A:GLU318 2.7 18.3 1.0
OE2 A:GLU318 2.8 15.3 1.0
CE1 A:HIS299 2.9 13.0 1.0
P A:PH0706 2.9 18.6 1.0
CD2 A:HIS295 3.0 14.8 1.0
CE1 A:HIS295 3.0 14.5 1.0
O5 A:PH0706 3.1 20.8 1.0
CD2 A:HIS299 3.1 13.4 1.0
CE2 A:TYR383 3.8 20.1 1.0
N2 A:PH0706 3.8 15.4 1.0
ND1 A:HIS299 4.0 14.0 1.0
C8 A:PH0706 4.1 19.6 1.0
ND1 A:HIS295 4.1 16.6 1.0
CG A:HIS295 4.1 15.8 1.0
OH A:TYR383 4.1 22.0 1.0
CG A:HIS299 4.1 14.5 1.0
CG A:GLU318 4.2 18.0 1.0
CG2 A:THR321 4.3 17.9 1.0
CZ A:TYR383 4.4 21.8 1.0
C9 A:PH0706 4.5 18.2 1.0
C21 A:PH0706 4.5 19.0 1.0
C10 A:PH0706 4.6 18.3 1.0
OE1 A:GLU271 4.6 21.9 1.0
CB A:THR321 4.6 14.7 1.0
C1 A:PH0706 4.7 21.2 1.0
CB A:GLU318 4.8 18.7 1.0
C27 A:PH0706 4.8 23.0 1.0
CD2 A:TYR383 4.8 20.1 1.0
O A:HOH724 4.8 22.9 1.0
OE2 A:GLU296 4.8 18.1 1.0
CA A:GLU318 4.9 18.6 1.0
C22 A:PH0706 4.9 20.8 1.0
OE2 A:GLU271 5.0 23.9 1.0
CD A:GLU271 5.0 23.7 1.0

Reference:

F.Tholander, A.Muroya, B.P.Roques, M.C.Fournie-Zaluski, M.M.Thunnissen, J.Z.Haeggstrom. Structure-Based Dissection of the Active Site Chemistry of Leukotriene A4 Hydrolase: Implications For M1 Aminopeptidases and Inhibitor Design. Chem.Biol. V. 15 920 2008.
ISSN: ISSN 1074-5521
PubMed: 18804029
DOI: 10.1016/J.CHEMBIOL.2008.07.018
Page generated: Wed Dec 16 03:51:34 2020

Last articles

Zn in 7M6U
Zn in 7NNG
Zn in 7NEE
Zn in 7NEU
Zn in 7M3K
Zn in 7KWD
Zn in 7KYH
Zn in 7KNG
Zn in 7KY2
Zn in 7KYF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy