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Zinc in PDB 7llq: 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: 7llq was solved by K.H.Lee, S.H.Lee, Y.M.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) 45.19 / 2.85
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 138.054, 138.054, 84.257, 90, 90, 120
R / Rfree (%) 20 / 22.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Substrate-Dependent Divergence of Leukotriene A4 Hydrolase Aminopeptidase Activity (pdb code 7llq). 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: 7llq:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 7llq

Go back to Zinc Binding Sites List in 7llq
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:22.8
occ:1.00
O A:28T703 1.3 15.9 1.0
OE1 A:GLU318 2.0 14.3 1.0
NE2 A:HIS299 2.0 12.4 1.0
NE2 A:HIS295 2.2 13.2 1.0
C A:28T703 2.5 14.6 1.0
CD A:GLU318 2.8 15.5 1.0
O A:HOH810 2.8 17.6 1.0
CE1 A:HIS299 3.0 12.6 1.0
OE2 A:GLU318 3.1 17.1 1.0
CD2 A:HIS299 3.1 11.7 1.0
CE1 A:HIS295 3.1 13.7 1.0
CA A:28T703 3.2 12.1 1.0
CD2 A:HIS295 3.2 12.6 1.0
H13 A:28T703 3.3 16.9 1.0
CE2 A:TYR383 3.7 13.4 1.0
CAH A:28T703 3.7 12.9 1.0
H10 A:28T703 3.8 15.1 1.0
N A:28T703 4.0 11.0 1.0
OH A:TYR383 4.1 14.6 1.0
ND1 A:HIS299 4.1 11.8 1.0
CG A:HIS299 4.2 12.3 1.0
H12 A:28T703 4.2 15.6 1.0
OE2 A:GLU271 4.2 14.2 1.0
OE1 A:GLU271 4.2 11.6 1.0
CAI A:28T703 4.2 12.6 1.0
CG A:GLU318 4.2 12.9 1.0
ND1 A:HIS295 4.3 13.6 1.0
CG2 A:THR321 4.3 11.7 1.0
CZ A:TYR383 4.3 13.9 1.0
CG A:HIS295 4.3 12.4 1.0
CB A:28T703 4.4 13.5 1.0
H20 A:28T703 4.4 20.9 1.0
H9 A:28T703 4.5 15.1 1.0
CD A:GLU271 4.5 11.3 1.0
H11 A:28T703 4.5 15.6 1.0
CB A:GLU318 4.7 12.7 1.0
CD2 A:TYR383 4.7 13.4 1.0
CA A:GLU318 4.7 12.8 1.0
CB A:THR321 4.7 12.1 1.0
H15 A:28T703 4.8 17.5 1.0
OE2 A:GLU296 4.8 12.3 1.0
H14 A:28T703 4.9 17.5 1.0

Zinc binding site 2 out of 3 in 7llq

Go back to Zinc Binding Sites List in 7llq
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:20.2
occ:1.00
O B:28T703 1.7 11.3 1.0
NE2 B:HIS299 2.0 15.1 1.0
OE1 B:GLU318 2.0 16.5 1.0
NE2 B:HIS295 2.3 16.2 1.0
C B:28T703 2.8 12.7 1.0
CD B:GLU318 2.8 16.6 1.0
CE1 B:HIS299 2.9 14.9 1.0
OE2 B:GLU318 3.0 19.8 1.0
CD2 B:HIS299 3.0 13.8 1.0
O B:HOH813 3.1 17.7 1.0
CE1 B:HIS295 3.2 16.1 1.0
CD2 B:HIS295 3.3 14.7 1.0
H12 B:28T703 3.4 19.9 1.0
H13 B:28T703 3.6 19.4 1.0
CA B:28T703 3.6 12.1 1.0
CE2 B:TYR383 3.6 14.8 1.0
H9 B:28T703 3.6 18.1 1.0
OH B:TYR383 3.7 16.9 1.0
CAH B:28T703 3.8 16.6 1.0
N B:28T703 3.8 11.0 1.0
H20 B:28T703 4.0 20.1 1.0
ND1 B:HIS299 4.0 14.4 1.0
CZ B:TYR383 4.1 16.0 1.0
CG B:HIS299 4.1 13.4 1.0
CG B:GLU318 4.2 13.0 1.0
CAI B:28T703 4.2 15.1 1.0
OE2 B:GLU271 4.2 17.5 1.0
ND1 B:HIS295 4.3 16.4 1.0
CG B:HIS295 4.4 13.1 1.0
OE1 B:GLU271 4.4 16.0 1.0
H10 B:28T703 4.5 18.1 1.0
CG2 B:THR321 4.6 13.1 1.0
CD B:GLU271 4.6 15.3 1.0
CD2 B:TYR383 4.6 15.0 1.0
H11 B:28T703 4.7 19.9 1.0
CB B:GLU318 4.7 13.6 1.0
CA B:GLU318 4.7 14.7 1.0
OE2 B:GLU296 4.8 13.9 1.0
CB B:THR321 4.9 12.9 1.0

Zinc binding site 3 out of 3 in 7llq

Go back to Zinc Binding Sites List in 7llq
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:29.8
occ:1.00
O C:28T703 1.0 28.6 1.0
OE1 C:GLU318 1.9 20.9 1.0
NE2 C:HIS299 2.1 20.4 1.0
NE2 C:HIS295 2.3 19.6 1.0
C C:28T703 2.3 25.9 1.0
CD C:GLU318 2.7 22.7 1.0
CE1 C:HIS299 2.9 18.7 1.0
OE2 C:GLU318 2.9 24.4 1.0
O C:HOH805 3.1 19.0 1.0
CD2 C:HIS299 3.2 18.6 1.0
CE1 C:HIS295 3.3 19.8 1.0
CD2 C:HIS295 3.3 19.1 1.0
CA C:28T703 3.4 27.6 1.0
CE2 C:TYR383 3.4 20.5 1.0
OH C:TYR383 3.6 21.5 1.0
CAH C:28T703 3.7 21.7 1.0
N C:28T703 3.7 27.5 1.0
CZ C:TYR383 4.0 19.8 1.0
ND1 C:HIS299 4.1 17.8 1.0
CG C:GLU318 4.1 18.4 1.0
CAI C:28T703 4.2 20.8 1.0
OE2 C:GLU271 4.2 24.6 1.0
CG C:HIS299 4.2 17.7 1.0
OE1 C:GLU271 4.3 22.0 1.0
ND1 C:HIS295 4.4 19.4 1.0
CG C:HIS295 4.4 19.3 1.0
CG2 C:THR321 4.4 17.2 1.0
CD2 C:TYR383 4.5 19.3 1.0
CB C:28T703 4.5 24.4 1.0
CD C:GLU271 4.5 23.3 1.0
CB C:GLU318 4.6 17.9 1.0
CA C:GLU318 4.7 17.0 1.0
CB C:THR321 4.8 16.2 1.0
OE2 C:GLU296 4.9 19.6 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: Sat Apr 8 00:28:52 2023

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