Zinc in PDB 5ijt: Human Peroxiredoxin 2 Oxidized (Ss)

All present enzymatic activity of Human Peroxiredoxin 2 Oxidized (Ss):
1.11.1.15;

The structure of Human Peroxiredoxin 2 Oxidized (Ss), PDB code: 5ijt was solved by A.C.Haynes, J.A.Bolduc, W.T.Lowther, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.46 / 2.15
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	50.014, 198.784, 116.523, 90.00, 96.28, 90.00
R / Rfree (%)	20.7 / 25.7

The binding sites of Zinc atom in the Human Peroxiredoxin 2 Oxidized (Ss) (pdb code 5ijt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Human Peroxiredoxin 2 Oxidized (Ss), PDB code: 5ijt:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Human Peroxiredoxin 2 Oxidized (Ss)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Peroxiredoxin 2 Oxidized (Ss) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:63.5 occ:1.00 OE2 B:GLU93 1.8 50.6 1.0 CD B:GLU93 2.7 66.1 1.0 OE1 B:GLU93 2.9 74.2 1.0 HZ1 B:LYS92 3.8 94.6 1.0 HD2 B:PRO90 4.0 60.9 1.0 CG B:GLU93 4.1 63.4 1.0 HG2 B:PRO90 4.1 71.5 1.0 HZ2 B:LYS92 4.2 94.6 1.0 HG3 B:GLU93 4.2 76.0 1.0 NZ B:LYS92 4.4 78.8 1.0 HG2 B:GLU93 4.5 76.0 1.0 HD3 E:PRO90 4.5 74.5 1.0 HG3 E:PRO90 4.7 81.2 1.0 CD B:PRO90 4.7 50.8 1.0 HZ3 B:LYS92 4.8 94.6 1.0 HD3 B:PRO90 4.8 60.9 1.0 CG B:PRO90 4.9 59.6 1.0 HB2 B:GLU93 5.0 74.4 1.0

Zinc binding site 2 out of 4 in the Human Peroxiredoxin 2 Oxidized (Ss)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Peroxiredoxin 2 Oxidized (Ss) within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn201 b:0.4 occ:1.00 OE1 F:GLU167 2.6 0.7 1.0 CD F:GLU167 3.0 92.1 1.0 OE2 F:GLU167 3.1 78.5 1.0 CG F:GLU167 4.1 83.5 1.0 HG3 F:GLU167 4.2 0.2 1.0 HG2 F:GLU167 4.4 0.2 1.0 ZN F:ZN202 4.9 0.1 1.0

Zinc binding site 3 out of 4 in the Human Peroxiredoxin 2 Oxidized (Ss)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Human Peroxiredoxin 2 Oxidized (Ss) within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn202 b:0.1 occ:1.00 NE2 F:HIS168 2.1 86.0 1.0 CE1 F:HIS168 2.8 89.3 1.0 HG2 F:GLU167 2.9 0.2 1.0 HE1 F:HIS168 2.9 0.2 1.0 OE1 F:GLU167 3.2 0.7 1.0 CD2 F:HIS168 3.2 86.7 1.0 HD2 F:HIS168 3.6 0.1 1.0 CG F:GLU167 3.8 83.5 1.0 CD F:GLU167 3.9 92.1 1.0 ND1 F:HIS168 4.0 79.4 1.0 CG F:HIS168 4.2 80.9 1.0 HG3 F:GLU167 4.3 0.2 1.0 HB3 F:GLU167 4.3 87.3 1.0 CB F:GLU167 4.6 72.7 1.0 HD1 F:HIS168 4.7 95.3 1.0 HD1 F:TYR164 4.8 85.8 1.0 ZN F:ZN201 4.9 0.4 1.0

Zinc binding site 4 out of 4 in the Human Peroxiredoxin 2 Oxidized (Ss)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Human Peroxiredoxin 2 Oxidized (Ss) within 5.0Å range: probe atom residue distance (Å) B Occ H:Zn201 b:0.6 occ:1.00 HA H:TYR164 2.9 67.8 1.0 HE2 H:HIS168 2.9 90.3 1.0 HB3 H:GLU167 3.3 88.6 1.0 HD2 H:HIS168 3.3 89.8 1.0 HG2 H:GLU167 3.5 0.6 1.0 NE2 H:HIS168 3.6 75.3 1.0 CD2 H:HIS168 3.8 74.9 1.0 CA H:TYR164 3.8 56.5 1.0 HB2 H:GLU167 3.9 88.6 1.0 CB H:GLU167 4.0 73.8 1.0 HD1 H:TYR164 4.2 81.8 1.0 HB2 H:TYR164 4.2 68.4 1.0 CG H:GLU167 4.2 91.3 1.0 N H:TYR164 4.3 51.3 1.0 O H:GLN163 4.3 55.0 1.0 CB H:TYR164 4.4 57.0 1.0 CD1 H:TYR164 4.5 68.2 1.0 C H:GLN163 4.5 56.3 1.0 CG H:TYR164 4.6 71.0 1.0 O H:TYR164 4.7 61.1 1.0 HG3 H:GLU167 4.8 0.6 1.0 HB3 H:GLN163 4.8 60.1 1.0 H H:TYR164 4.8 61.6 1.0 C H:TYR164 4.8 64.2 1.0 CE1 H:HIS168 4.8 71.4 1.0 H H:GLU167 5.0 70.8 1.0

J.A.Bolduc, K.J.Nelson, A.C.Haynes, J.Lee, J.A.Reisz, A.H.Graff, J.E.Clodfelter, D.Parsonage, L.B.Poole, C.M.Furdui, W.T.Lowther. Novel Hyperoxidation Resistance Motifs in 2-Cys Peroxiredoxins. J. Biol. Chem. V. 293 11901 2018.
ISSN: ESSN 1083-351X
PubMed: 29884768
DOI: 10.1074/JBC.RA117.001690