Zinc in PDB 7kze: Substrate-Dependent Divergence of Leukotriene A4 Hydrolase Aminopeptidase Activity

Enzymatic activity of Substrate-Dependent Divergence of Leukotriene A4 Hydrolase Aminopeptidase Activity

All present enzymatic activity of Substrate-Dependent Divergence of Leukotriene A4 Hydrolase Aminopeptidase Activity:
3.3.2.6; 3.4.11.4;

Protein crystallography data

The structure of Substrate-Dependent Divergence of Leukotriene A4 Hydrolase Aminopeptidase Activity, PDB code: 7kze was solved by K.H.Lee, Y.Shim, M.Paige, S.M.Noble, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 53.84 / 2.90
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 139.888, 139.888, 84.343, 90, 90, 120
R / Rfree (%) 19.5 / 20.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Substrate-Dependent Divergence of Leukotriene A4 Hydrolase Aminopeptidase Activity (pdb code 7kze). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Substrate-Dependent Divergence of Leukotriene A4 Hydrolase Aminopeptidase Activity, PDB code: 7kze:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 7kze

Go back to Zinc Binding Sites List in 7kze
Zinc binding site 1 out of 3 in the Substrate-Dependent Divergence of Leukotriene A4 Hydrolase Aminopeptidase Activity


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Substrate-Dependent Divergence of Leukotriene A4 Hydrolase Aminopeptidase Activity within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:17.7
occ:1.00
OE1 A:GLU318 1.9 15.7 1.0
NE2 A:HIS295 2.2 15.6 1.0
NE2 A:HIS299 2.3 15.2 1.0
O A:HOH801 2.5 17.6 1.0
CD A:GLU318 2.6 14.8 1.0
OE2 A:GLU318 2.7 15.3 1.0
CD2 A:HIS295 2.9 14.1 1.0
O A:HOH860 3.1 17.6 1.0
CD2 A:HIS299 3.1 14.7 1.0
CE1 A:HIS295 3.3 13.9 1.0
CE1 A:HIS299 3.3 14.3 1.0
CE2 A:TYR383 3.6 16.6 1.0
OH A:TYR383 3.7 17.4 1.0
OE1 A:GLU271 3.7 17.5 1.0
O A:HOH956 3.9 17.4 1.0
CG A:GLU318 4.0 15.2 1.0
CZ A:TYR383 4.1 17.1 1.0
O A:HOH807 4.1 17.8 1.0
CG A:HIS295 4.2 14.5 1.0
O A:HOH994 4.2 19.7 1.0
ND1 A:HIS295 4.3 14.7 1.0
CG A:HIS299 4.3 14.3 1.0
ND1 A:HIS299 4.4 13.9 1.0
OE2 A:GLU296 4.4 16.7 1.0
CG2 A:THR321 4.6 14.0 1.0
CD2 A:TYR383 4.6 16.6 1.0
CD A:GLU271 4.6 16.3 1.0
CB A:GLU318 4.7 14.6 1.0
O A:HOH910 4.7 17.5 1.0
OE1 A:GLU296 4.8 15.8 1.0
CA A:GLU318 4.9 14.9 1.0
OE2 A:GLU271 4.9 16.4 1.0
CD A:GLU296 4.9 16.3 1.0
CB A:THR321 5.0 14.2 1.0

Zinc binding site 2 out of 3 in 7kze

Go back to Zinc Binding Sites List in 7kze
Zinc binding site 2 out of 3 in the Substrate-Dependent Divergence of Leukotriene A4 Hydrolase Aminopeptidase Activity


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Substrate-Dependent Divergence of Leukotriene A4 Hydrolase Aminopeptidase Activity within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn701

b:27.3
occ:1.00
OE1 B:GLU318 1.9 23.1 1.0
NE2 B:HIS299 2.2 22.6 1.0
NE2 B:HIS295 2.3 22.2 1.0
OE2 B:GLU318 2.5 24.2 1.0
CD B:GLU318 2.5 23.3 1.0
O B:HOH895 3.0 21.6 1.0
CD2 B:HIS299 3.1 22.1 1.0
CD2 B:HIS295 3.1 21.4 1.0
CE1 B:HIS299 3.3 22.3 1.0
CE1 B:HIS295 3.4 21.8 1.0
O B:HOH821 3.4 26.3 1.0
OH B:TYR383 3.7 24.0 1.0
CE2 B:TYR383 3.7 24.2 1.0
OE1 B:GLU271 3.9 26.0 1.0
CG B:GLU318 4.0 23.1 1.0
CZ B:TYR383 4.1 24.2 1.0
CG B:HIS299 4.3 21.6 1.0
ND1 B:HIS299 4.3 21.4 1.0
CG B:HIS295 4.3 21.7 1.0
ND1 B:HIS295 4.4 22.1 1.0
OE2 B:GLU271 4.4 25.1 1.0
CD B:GLU271 4.4 25.6 1.0
OE1 B:GLU296 4.6 24.2 1.0
CB B:GLU318 4.7 22.9 1.0
CG2 B:THR321 4.8 21.3 1.0
CD2 B:TYR383 4.8 24.7 1.0
O B:HOH856 4.9 23.6 1.0
OE2 B:GLU296 4.9 23.4 1.0
CA B:GLU318 4.9 22.7 1.0

Zinc binding site 3 out of 3 in 7kze

Go back to Zinc Binding Sites List in 7kze
Zinc binding site 3 out of 3 in the Substrate-Dependent Divergence of Leukotriene A4 Hydrolase Aminopeptidase Activity


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Substrate-Dependent Divergence of Leukotriene A4 Hydrolase Aminopeptidase Activity within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn701

b:21.9
occ:1.00
OE1 C:GLU318 1.9 18.5 1.0
NE2 C:HIS299 2.1 18.4 1.0
NE2 C:HIS295 2.1 18.6 1.0
O C:HOH876 2.4 18.4 1.0
CD C:GLU318 2.6 17.4 1.0
OE2 C:GLU318 2.7 17.7 1.0
CD2 C:HIS299 2.9 18.1 1.0
CD2 C:HIS295 3.0 18.2 1.0
CE1 C:HIS295 3.2 17.8 1.0
CE1 C:HIS299 3.2 17.4 1.0
O C:HOH848 3.6 20.0 1.0
CE2 C:TYR383 3.7 18.4 1.0
OH C:TYR383 3.8 18.7 1.0
OE1 C:GLU271 3.9 18.8 1.0
CG C:GLU318 4.1 17.9 1.0
CG C:HIS299 4.1 17.2 1.0
CZ C:TYR383 4.1 18.1 1.0
O C:HOH911 4.1 19.7 1.0
CG C:HIS295 4.2 18.3 1.0
ND1 C:HIS299 4.2 17.9 1.0
ND1 C:HIS295 4.2 18.2 1.0
CD C:GLU271 4.4 18.4 1.0
CG2 C:THR321 4.5 18.2 1.0
OE2 C:GLU271 4.5 18.5 1.0
OE2 C:GLU296 4.6 19.5 1.0
CB C:GLU318 4.7 18.8 1.0
CD2 C:TYR383 4.7 18.6 1.0
O C:HOH874 4.8 18.3 1.0
CA C:GLU318 4.8 19.1 1.0
OE1 C:GLU296 4.8 18.7 1.0
CB C:THR321 4.9 18.6 1.0

Reference:

K.H.Lee, N.F.Ali, S.H.Lee, Z.Zhang, M.Burdick, Z.J.Beaulac, G.Petruncio, L.Li, J.Xiang, E.M.Chung, K.W.Foreman, S.M.Noble, Y.M.Shim, M.Paige. Substrate-Dependent Modulation of the Leukotriene A 4 Hydrolase Aminopeptidase Activity and Effect in A Murine Model of Acute Lung Inflammation. Sci Rep V. 12 9443 2022.
ISSN: ESSN 2045-2322
PubMed: 35676292
DOI: 10.1038/S41598-022-13238-6
Page generated: Tue Oct 29 22:34:44 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy