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Zinc in PDB 4r7l: Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor H1

Enzymatic activity of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor H1

All present enzymatic activity of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor H1:
3.3.2.6;

Protein crystallography data

The structure of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor H1, PDB code: 4r7l was solved by P.Ouyang, K.Cui, W.Lu, J.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.19 / 1.66
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 77.916, 87.134, 99.285, 90.00, 90.00, 90.00
R / Rfree (%) 15.3 / 18.5

Other elements in 4r7l:

The structure of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor H1 also contains other interesting chemical elements:

Ytterbium (Yb) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor H1 (pdb code 4r7l). 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 Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor H1, PDB code: 4r7l:

Zinc binding site 1 out of 1 in 4r7l

Go back to Zinc Binding Sites List in 4r7l
Zinc binding site 1 out of 1 in the Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor H1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human Leukotriene A4 Hydrolase in Complex with Inhibitor H1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:12.0
occ:1.00
 O2 A:SHH709 2.0 12.3 1.0
NE2 A:HIS299 2.1 11.7 1.0
OE1 A:GLU318 2.1 12.2 1.0
CE1 A:HIS295 2.1 9.0 1.0
O1 A:SHH709 2.2 12.9 1.0
C1 A:SHH709 2.8 14.4 1.0
CD A:GLU318 2.8 11.6 1.0
N1 A:SHH709 2.9 13.4 1.0
OE2 A:GLU318 2.9 13.3 1.0
CE1 A:HIS299 3.0 10.3 1.0
NE2 A:HIS295 3.0 13.9 1.0
ND1 A:HIS295 3.1 12.4 1.0
CD2 A:HIS299 3.1 10.3 1.0
O A:HOH801 3.4 13.0 1.0
CE2 A:TYR383 4.0 12.2 1.0
OE1 A:GLU271 4.1 12.0 1.0
ND1 A:HIS299 4.1 10.8 1.0
OH A:TYR383 4.2 12.7 1.0
CG A:HIS299 4.2 9.8 1.0
CD2 A:HIS295 4.2 9.1 1.0
CG A:HIS295 4.2 10.6 1.0
C2 A:SHH709 4.3 13.6 1.0
CG A:GLU318 4.3 10.9 1.0
OE1 A:GLU296 4.3 12.6 1.0
CZ A:TYR383 4.5 12.1 1.0
CG2 A:THR321 4.6 11.2 1.0
CD A:GLU271 4.7 13.3 1.0
O A:HOH1214 4.8 12.7 1.0
OE2 A:GLU296 4.8 12.7 1.0
OE2 A:GLU271 4.8 13.1 1.0
CB A:GLU318 4.8 12.0 1.0
C1 A:GOL704 4.9 27.5 1.0
CD A:GLU296 4.9 12.9 1.0
C3 A:SHH709 5.0 14.6 1.0
CD2 A:TYR383 5.0 12.5 1.0
CB A:THR321 5.0 11.2 1.0

Reference:

P.Ouyang, K.Cui, W.Lu, J.Huang. Human Leukotriene A4 Hydrolase in Complex with Saha To Be Published.
Page generated: Wed Dec 16 05:44:58 2020

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