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Zinc in PDB 6o5h: The Effect of Modifier Structure on the Activation of Leukotriene A4 Hydrolase Aminopeptidase Activity.

Enzymatic activity of The Effect of Modifier Structure on the Activation of Leukotriene A4 Hydrolase Aminopeptidase Activity.

All present enzymatic activity of The Effect of Modifier Structure on the Activation of Leukotriene A4 Hydrolase Aminopeptidase Activity.:
3.3.2.6;

Protein crystallography data

The structure of The Effect of Modifier Structure on the Activation of Leukotriene A4 Hydrolase Aminopeptidase Activity., PDB code: 6o5h was solved by S.M.Noble, K.H.Lee, M.Paige, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 120.95 / 2.84
Space group P 32
Cell size a, b, c (Å), α, β, γ (°) 139.663, 139.663, 84.149, 90.00, 90.00, 120.00
R / Rfree (%) 21.9 / 22.9

Zinc Binding Sites:

The binding sites of Zinc atom in the The Effect of Modifier Structure on the Activation of Leukotriene A4 Hydrolase Aminopeptidase Activity. (pdb code 6o5h). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the The Effect of Modifier Structure on the Activation of Leukotriene A4 Hydrolase Aminopeptidase Activity., PDB code: 6o5h:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 6o5h

Go back to Zinc Binding Sites List in 6o5h
Zinc binding site 1 out of 3 in the The Effect of Modifier Structure on the Activation 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 The Effect of Modifier Structure on the Activation of Leukotriene A4 Hydrolase Aminopeptidase Activity. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn702

b:35.6
occ:1.00
OE1 A:GLU318 2.0 34.8 1.0
OE2 A:GLU318 2.2 62.1 1.0
NE2 A:HIS295 2.3 20.4 1.0
O A:HOH856 2.3 24.2 1.0
CD A:GLU318 2.3 35.5 1.0
NE2 A:HIS299 2.4 25.1 1.0
CD2 A:HIS295 3.1 21.6 1.0
CE2 A:TYR383 3.2 36.2 1.0
CD2 A:HIS299 3.3 25.1 1.0
CE1 A:HIS295 3.3 22.3 1.0
OH A:TYR383 3.4 56.9 1.0
CE1 A:HIS299 3.4 25.1 1.0
CZ A:TYR383 3.7 39.5 1.0
CG A:GLU318 3.8 32.0 1.0
OE1 A:GLU271 4.2 31.0 1.0
CG A:HIS295 4.3 20.6 1.0
CD2 A:TYR383 4.3 34.8 1.0
ND1 A:HIS295 4.4 21.4 1.0
CG A:HIS299 4.5 24.4 1.0
OE2 A:GLU271 4.5 26.0 1.0
ND1 A:HIS299 4.5 24.4 1.0
CB A:GLU318 4.6 29.6 1.0
CD A:GLU271 4.6 28.2 1.0
OE2 A:GLU296 4.7 21.6 1.0
OE1 A:GLU296 4.9 23.5 1.0
CA A:GLU318 5.0 26.5 1.0

Zinc binding site 2 out of 3 in 6o5h

Go back to Zinc Binding Sites List in 6o5h
Zinc binding site 2 out of 3 in the The Effect of Modifier Structure on the Activation 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 The Effect of Modifier Structure on the Activation of Leukotriene A4 Hydrolase Aminopeptidase Activity. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn702

b:26.5
occ:1.00
OE1 B:GLU318 1.8 26.8 1.0
NE2 B:HIS295 2.2 19.9 1.0
OE2 B:GLU318 2.3 40.2 1.0
O B:HOH860 2.3 20.3 1.0
CD B:GLU318 2.3 32.4 1.0
NE2 B:HIS299 2.3 21.9 1.0
CD2 B:HIS295 3.2 17.3 1.0
CE1 B:HIS295 3.2 19.5 1.0
CE1 B:HIS299 3.2 21.8 1.0
OH B:TYR383 3.3 42.7 1.0
CD2 B:HIS299 3.3 21.0 1.0
CE2 B:TYR383 3.4 30.7 1.0
CG B:GLU318 3.7 26.6 1.0
CZ B:TYR383 3.8 32.1 1.0
OE1 B:GLU271 4.1 21.4 1.0
ND1 B:HIS295 4.3 18.6 1.0
CG B:HIS295 4.3 16.5 1.0
ND1 B:HIS299 4.4 20.8 1.0
CG B:HIS299 4.5 19.7 1.0
CB B:GLU318 4.5 23.5 1.0
CD2 B:TYR383 4.6 29.0 1.0
OE2 B:GLU271 4.6 16.1 1.0
OE2 B:GLU296 4.6 16.0 1.0
CD B:GLU271 4.6 17.8 1.0
O B:HOH821 4.7 31.9 1.0
CA B:GLU318 4.9 21.6 1.0
CG2 B:THR321 4.9 15.6 1.0

Zinc binding site 3 out of 3 in 6o5h

Go back to Zinc Binding Sites List in 6o5h
Zinc binding site 3 out of 3 in the The Effect of Modifier Structure on the Activation 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 The Effect of Modifier Structure on the Activation of Leukotriene A4 Hydrolase Aminopeptidase Activity. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn702

b:29.0
occ:1.00
OE1 C:GLU318 2.2 25.3 1.0
OE2 C:GLU318 2.3 43.1 1.0
NE2 C:HIS299 2.3 19.1 1.0
NE2 C:HIS295 2.4 19.3 1.0
CD C:GLU318 2.5 27.7 1.0
CD2 C:HIS295 3.1 19.6 1.0
CD2 C:HIS299 3.2 19.8 1.0
CE1 C:HIS299 3.4 19.9 1.0
OH C:TYR383 3.4 26.6 1.0
CE1 C:HIS295 3.5 20.1 1.0
CE2 C:TYR383 3.6 25.6 1.0
CZ C:TYR383 3.9 26.5 1.0
OE1 C:GLU271 3.9 20.6 1.0
CG C:GLU318 4.0 23.5 1.0
CG C:HIS295 4.3 19.7 1.0
CG C:HIS299 4.4 18.8 1.0
OE2 C:GLU271 4.4 19.4 1.0
OE2 C:GLU296 4.4 19.2 1.0
ND1 C:HIS299 4.4 18.4 1.0
CD C:GLU271 4.5 18.8 1.0
ND1 C:HIS295 4.5 19.7 1.0
CD2 C:TYR383 4.7 25.0 1.0
OE1 C:GLU296 4.8 20.1 1.0
CB C:GLU318 4.9 22.6 1.0
CD C:GLU296 5.0 20.2 1.0

Reference:

K.H.Lee, G.Petruncio, A.Shim, M.Burdick, Z.Zhang, Y.M.Shim, S.M.Noble, M.Paige. Effect of Modifier Structure on the Activation of Leukotriene A4HYDROLASE Aminopeptidase Activity. J.Med.Chem. 2019.
ISSN: ISSN 0022-2623
PubMed: 31751136
DOI: 10.1021/ACS.JMEDCHEM.9B00663
Page generated: Tue Oct 29 04:06:29 2024

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