Zinc in PDB 4c6o: Crystal Structure of the Dihydroorotase Domain of Human Cad C1613S Mutant in Apo-Form at pH 6.0

All present enzymatic activity of Crystal Structure of the Dihydroorotase Domain of Human Cad C1613S Mutant in Apo-Form at pH 6.0:
3.5.2.3;

The structure of Crystal Structure of the Dihydroorotase Domain of Human Cad C1613S Mutant in Apo-Form at pH 6.0, PDB code: 4c6o was solved by S.Ramon-Maiques, N.Lallous, A.Grande-Garcia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.927 / 1.65
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.120, 159.420, 61.470, 90.00, 90.00, 90.00
R / Rfree (%)	11.47 / 15.71

The binding sites of Zinc atom in the Crystal Structure of the Dihydroorotase Domain of Human Cad C1613S Mutant in Apo-Form at pH 6.0 (pdb code 4c6o). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Dihydroorotase Domain of Human Cad C1613S Mutant in Apo-Form at pH 6.0, PDB code: 4c6o:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Dihydroorotase Domain of Human Cad C1613S Mutant in Apo-Form at pH 6.0


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 Dihydroorotase Domain of Human Cad C1613S Mutant in Apo-Form at pH 6.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2822 b:18.9 occ:0.72 NE2 A:HIS1471 2.0 15.6 1.0 NE2 A:HIS1473 2.0 17.2 1.0 O A:HOH2078 2.1 18.8 1.0 OD1 A:ASP1686 2.2 17.2 1.0 OQ1 A:KCX1556 2.2 20.1 1.0 CE1 A:HIS1473 3.0 17.0 1.0 CE1 A:HIS1471 3.0 19.3 1.0 CD2 A:HIS1471 3.0 15.0 1.0 CX A:KCX1556 3.1 18.3 1.0 CG A:ASP1686 3.1 16.1 1.0 HE1 A:HIS1473 3.1 20.4 1.0 CD2 A:HIS1473 3.1 19.1 1.0 HE1 A:HIS1471 3.2 23.2 1.0 HD2 A:HIS1471 3.2 18.0 1.0 HD2 A:HIS1473 3.3 23.0 1.0 ZN A:ZN2823 3.4 19.8 0.7 OQ2 A:KCX1556 3.4 19.6 1.0 HG3 A:MET1503 3.4 20.9 1.0 OD2 A:ASP1686 3.4 19.5 1.0 O A:HOH2380 3.9 45.9 1.0 HD2 A:HIS1614 4.0 21.8 1.0 ND1 A:HIS1471 4.1 20.7 1.0 HA A:ASP1686 4.1 18.4 1.0 ND1 A:HIS1473 4.1 17.4 1.0 CG A:HIS1471 4.1 15.2 1.0 HH A:TYR1558 4.1 21.6 1.0 HZ A:KCX1556 4.2 20.5 1.0 CG A:HIS1473 4.2 17.5 1.0 NZ A:KCX1556 4.2 17.1 1.0 HE1 A:TYR1558 4.3 22.0 1.0 CB A:ASP1686 4.4 14.7 1.0 CG A:MET1503 4.4 17.4 1.0 NE2 A:HIS1614 4.4 17.0 1.0 H A:FMT2824 4.4 46.7 0.5 CD2 A:HIS1614 4.5 18.1 1.0 HB2 A:ASP1686 4.6 17.6 1.0 HE1 A:MET1503 4.6 22.6 1.0 CA A:ASP1686 4.7 15.4 1.0 OH A:TYR1558 4.8 18.0 1.0 HG2 A:MET1503 4.8 20.9 1.0 HB3 A:ALA1688 4.9 21.0 1.0 HD1 A:HIS1471 4.9 24.8 1.0 HD1 A:HIS1473 4.9 20.9 1.0 HB2 A:MET1503 4.9 18.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Dihydroorotase Domain of Human Cad C1613S Mutant in Apo-Form at pH 6.0


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 Dihydroorotase Domain of Human Cad C1613S Mutant in Apo-Form at pH 6.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2823 b:19.8 occ:0.68 OQ2 A:KCX1556 1.9 19.6 1.0 NE2 A:HIS1614 2.0 17.0 1.0 ND1 A:HIS1590 2.0 19.5 1.0 O A:HOH2078 2.0 18.8 1.0 CX A:KCX1556 2.9 18.3 1.0 CE1 A:HIS1590 2.9 19.1 1.0 CE1 A:HIS1614 2.9 17.1 1.0 HB2 A:HIS1590 3.0 16.8 1.0 HE1 A:HIS1590 3.0 22.9 1.0 HE1 A:HIS1614 3.1 20.5 1.0 CG A:HIS1590 3.1 17.1 1.0 CD2 A:HIS1614 3.1 18.1 1.0 HE1 A:HIS1471 3.1 23.2 1.0 OQ1 A:KCX1556 3.2 20.1 1.0 HD2 A:HIS1614 3.3 21.8 1.0 ZN A:ZN2822 3.4 18.9 0.7 CB A:HIS1590 3.5 14.0 1.0 O A:HOH2380 3.8 45.9 1.0 CE1 A:HIS1471 3.8 19.3 1.0 HE1 A:TYR1558 3.9 22.0 1.0 NE2 A:HIS1590 4.0 19.9 1.0 NE2 A:HIS1471 4.0 15.6 1.0 ND1 A:HIS1614 4.1 20.7 1.0 CD2 A:HIS1590 4.1 19.6 1.0 OG A:SER1613 4.1 17.2 0.1 OD2 A:ASP1686 4.2 19.5 1.0 HA A:HIS1590 4.2 15.5 1.0 NZ A:KCX1556 4.2 17.1 1.0 CG A:HIS1614 4.2 18.7 1.0 HB3 A:HIS1590 4.2 16.8 1.0 HB2 A:SER1613 4.3 19.9 0.9 HB3 A:SER1613 4.3 19.9 0.9 HE3 A:KCX1556 4.4 20.4 1.0 HB3 A:SER1613 4.4 19.7 0.1 HD3 A:PRO1662 4.4 23.2 1.0 CA A:HIS1590 4.5 12.9 1.0 HE2 A:KCX1556 4.5 20.4 1.0 CE1 A:TYR1558 4.6 18.4 1.0 CE A:KCX1556 4.6 17.0 1.0 HG A:SER1613 4.6 20.7 0.1 HZ A:KCX1556 4.7 20.5 1.0 OD1 A:ASP1686 4.7 17.2 1.0 HD1 A:TYR1558 4.7 20.2 1.0 O A:ARG1661 4.7 27.9 1.0 CB A:SER1613 4.7 16.6 0.9 CG A:ASP1686 4.7 16.1 1.0 HE2 A:HIS1590 4.8 23.9 1.0 CB A:SER1613 4.8 16.4 0.1 HD1 A:HIS1614 4.8 24.8 1.0 HD2 A:HIS1590 5.0 23.6 1.0

A.Grande-Garcia, N.Lallous, C.Diaz-Tejada, S.Ramon-Maiques. Structure, Functional Characterization and Evolution of the Dihydroorotase Domain of Human Cad. Structure V. 22 185 2014.
ISSN: ISSN 0969-2126
PubMed: 24332717
DOI: 10.1016/J.STR.2013.10.016