Zinc in PDB 5chc: Crystal Structure of the Perchlorate Reductase Pcrab - Substrate Analog SEO3 Bound - From Azospira Suillum Ps

The structure of Crystal Structure of the Perchlorate Reductase Pcrab - Substrate Analog SEO3 Bound - From Azospira Suillum Ps, PDB code: 5chc was solved by C.-L.Tsai, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.52 / 2.38
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	133.926, 176.022, 193.691, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 22.7

The structure of Crystal Structure of the Perchlorate Reductase Pcrab - Substrate Analog SEO3 Bound - From Azospira Suillum Ps also contains other interesting chemical elements:

Molybdenum	(Mo)	3 atoms
Iron	(Fe)	57 atoms
Sodium	(Na)	8 atoms

The binding sites of Zinc atom in the Crystal Structure of the Perchlorate Reductase Pcrab - Substrate Analog SEO3 Bound - From Azospira Suillum Ps (pdb code 5chc). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the Perchlorate Reductase Pcrab - Substrate Analog SEO3 Bound - From Azospira Suillum Ps, PDB code: 5chc:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of the Perchlorate Reductase Pcrab - Substrate Analog SEO3 Bound - From Azospira Suillum Ps


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 the Perchlorate Reductase Pcrab - Substrate Analog SEO3 Bound - From Azospira Suillum Ps within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1017 b:57.5 occ:1.00 O A:HOH1166 2.3 39.4 1.0 NE2 A:HIS81 2.4 36.3 1.0 O3 A:SO31014 2.5 50.3 1.0 O B:HOH506 2.6 37.9 1.0 O2 A:SO31014 2.6 54.1 1.0 S A:SO31014 2.7 82.7 1.0 CD2 A:HIS81 3.1 28.2 1.0 CE1 A:HIS81 3.6 29.4 1.0 NZ B:LYS33 3.8 32.3 1.0 O A:MET52 4.0 28.3 1.0 O A:HOH1177 4.0 37.9 1.0 O1 A:SO31014 4.1 62.0 1.0 CG A:HIS81 4.4 26.8 1.0 CD B:LYS33 4.5 32.3 1.0 OD1 A:ASP82 4.5 34.2 1.0 ND1 A:HIS81 4.6 34.1 1.0 CE B:LYS33 4.8 30.0 1.0 C A:MET52 4.9 30.7 1.0 O A:VAL51 5.0 32.1 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of the Perchlorate Reductase Pcrab - Substrate Analog SEO3 Bound - From Azospira Suillum Ps


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Perchlorate Reductase Pcrab - Substrate Analog SEO3 Bound - From Azospira Suillum Ps within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1013 b:82.7 occ:1.00 O2 C:SO31010 2.1 65.2 1.0 S C:SO31010 2.4 83.6 1.0 O D:HOH527 2.4 51.0 1.0 NE2 C:HIS81 2.5 41.6 1.0 O3 C:SO31010 2.6 69.0 1.0 CD2 C:HIS81 3.2 44.5 1.0 CE1 C:HIS81 3.7 40.1 1.0 NZ D:LYS33 3.8 38.0 1.0 O1 C:SO31010 3.8 60.8 1.0 O C:MET52 4.1 46.0 1.0 CD D:LYS33 4.2 41.3 1.0 OD1 C:ASP82 4.5 43.4 1.0 CG C:HIS81 4.5 41.5 1.0 CE D:LYS33 4.5 40.7 1.0 CG2 D:THR37 4.5 59.6 1.0 ND1 C:HIS81 4.7 39.8 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of the Perchlorate Reductase Pcrab - Substrate Analog SEO3 Bound - From Azospira Suillum Ps


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Perchlorate Reductase Pcrab - Substrate Analog SEO3 Bound - From Azospira Suillum Ps within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn1013 b:52.2 occ:1.00 S E:SO31009 2.3 86.4 1.0 NE2 E:HIS81 2.3 31.0 1.0 O3 E:SO31009 2.4 52.8 1.0 O2 E:SO31009 2.8 52.9 1.0 O F:HOH565 2.8 30.4 1.0 CD2 E:HIS81 3.0 31.0 1.0 CE1 E:HIS81 3.5 26.2 1.0 O1 E:SO31009 3.6 70.1 1.0 O E:MET52 3.9 30.8 1.0 NZ F:LYS33 4.1 29.2 1.0 CG E:HIS81 4.2 28.5 1.0 OD1 E:ASP82 4.4 28.7 1.0 ND1 E:HIS81 4.4 30.6 1.0 CD F:LYS33 4.5 31.4 1.0 CE F:LYS33 4.8 28.7 1.0 C E:MET52 4.8 29.4 1.0 O E:VAL51 4.9 32.7 1.0

M.D.Youngblut, C.L.Tsai, I.C.Clark, H.K.Carlson, A.P.Maglaqui, P.S.Gau-Pan, S.A.Redford, A.Wong, J.A.Tainer, J.D.Coates. Perchlorate Reductase Is Distinguished By Active Site Aromatic Gate Residues. J.Biol.Chem. V. 291 9190 2016.
ISSN: ESSN 1083-351X
PubMed: 26940877
DOI: 10.1074/JBC.M116.714618