Zinc in PDB 5nia: Crystal Structure of Human LTA4H Mutant D375N in Open Conformation (Crystal Form I)

All present enzymatic activity of Crystal Structure of Human LTA4H Mutant D375N in Open Conformation (Crystal Form I):
3.3.2.6;

The structure of Crystal Structure of Human LTA4H Mutant D375N in Open Conformation (Crystal Form I), PDB code: 5nia was solved by A.Stsiapanava, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.17 / 1.76
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	153.000, 153.000, 74.880, 90.00, 90.00, 120.00
R / Rfree (%)	18 / 20.7

The binding sites of Zinc atom in the Crystal Structure of Human LTA4H Mutant D375N in Open Conformation (Crystal Form I) (pdb code 5nia). 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 Crystal Structure of Human LTA4H Mutant D375N in Open Conformation (Crystal Form I), PDB code: 5nia:

Zinc binding site 1 out of 1 in the Crystal Structure of Human LTA4H Mutant D375N in Open Conformation (Crystal Form I)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human LTA4H Mutant D375N in Open Conformation (Crystal Form I) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn900 b:31.6 occ:1.00 NE2 A:HIS299 2.1 26.9 1.0 NE2 A:HIS295 2.1 26.5 1.0 OE2 A:GLU318 2.1 31.3 0.5 OE1 A:GLU318 2.1 27.5 0.5 OE1 A:GLU318 2.1 28.3 0.6 O A:HOH1162 2.2 36.7 1.0 O A:HOH1122 2.2 32.5 1.0 O A:HOH1011 2.4 24.5 0.6 CD A:GLU318 2.4 25.4 0.5 CE1 A:HIS299 3.0 24.6 1.0 CD A:GLU318 3.0 28.6 0.6 CD2 A:HIS295 3.1 25.6 1.0 HE1 A:HIS299 3.1 29.5 1.0 CE1 A:HIS295 3.1 23.2 1.0 CD2 A:HIS299 3.1 24.2 1.0 HD2 A:HIS295 3.2 30.8 1.0 OE2 A:GLU318 3.3 34.4 0.6 HE1 A:HIS295 3.3 27.9 1.0 HD2 A:HIS299 3.4 29.0 1.0 HG21 A:THR321 3.9 29.7 1.0 CG A:GLU318 3.9 30.1 0.5 O A:HOH1011 4.0 23.6 0.5 HE1 A:TYR383 4.0 43.2 0.5 ND1 A:HIS299 4.1 25.2 1.0 OE1 A:GLU271 4.1 27.5 1.0 ND1 A:HIS295 4.2 24.4 1.0 CG A:HIS295 4.2 24.7 1.0 CG A:HIS299 4.2 20.9 1.0 O A:HOH1100 4.2 38.9 0.9 HA A:GLU318 4.2 31.1 0.6 HG2 A:GLU318 4.3 36.1 0.5 HG2 A:GLU318 4.3 37.3 0.6 CG A:GLU318 4.3 31.1 0.6 HA A:GLU318 4.3 31.0 0.5 HG3 A:GLU318 4.4 36.1 0.5 O A:HOH1297 4.4 52.6 1.0 O A:HOH1016 4.4 50.5 1.0 OE2 A:GLU271 4.5 28.9 1.0 HB3 A:GLU318 4.5 29.9 0.5 CD A:GLU271 4.6 28.4 1.0 CE1 A:TYR383 4.6 36.0 0.5 HZ A:PHE314 4.7 42.2 1.0 CG2 A:THR321 4.7 24.8 1.0 CB A:GLU318 4.7 24.9 0.5 HB A:THR321 4.7 30.5 1.0 HG22 A:THR321 4.8 29.7 1.0 HD1 A:HIS299 4.9 30.2 1.0 HG3 A:GLU318 4.9 37.3 0.6 HE1 A:TYR383 4.9 42.3 0.6 HD1 A:TYR383 4.9 45.0 0.6 HD1 A:HIS295 5.0 29.3 1.0

A.Stsiapanava, B.Samuelsson, J.Z.Haeggstrom. Capturing LTA4 Hydrolase in Action: Insights to the Chemistry and Dynamics of Chemotactic LTB4 Synthesis. Proc. Natl. Acad. Sci. V. 114 9689 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28827365
DOI: 10.1073/PNAS.1710850114