Zinc in PDB 5ynz: Crystal Structure of the Dihydroorotase Domain (K1556A) of Human Cad

All present enzymatic activity of Crystal Structure of the Dihydroorotase Domain (K1556A) of Human Cad:
2.1.3.2; 3.5.2.3; 6.3.5.5;

The structure of Crystal Structure of the Dihydroorotase Domain (K1556A) of Human Cad, PDB code: 5ynz was solved by Y.H.Huang, K.L.Chen, J.H.Cheng, C.Y.Huang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.81 / 2.77
Space group	C 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	88.841, 108.630, 99.219, 90.00, 90.00, 90.00
R / Rfree (%)	22.6 / 28.9

The binding sites of Zinc atom in the Crystal Structure of the Dihydroorotase Domain (K1556A) of Human Cad (pdb code 5ynz). 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 the Dihydroorotase Domain (K1556A) of Human Cad, PDB code: 5ynz:

Zinc binding site 1 out of 1 in the Crystal Structure of the Dihydroorotase Domain (K1556A) of Human Cad


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 (K1556A) of Human Cad within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1901 b:70.6 occ:1.00 NE2 A:HIS1473 2.1 61.5 1.0 OD1 A:ASP1686 2.2 61.7 1.0 NE2 A:HIS1471 2.2 59.3 1.0 CE1 A:HIS1473 2.8 63.4 1.0 CE1 A:HIS1471 3.0 61.3 1.0 NE2 A:HIS1590 3.1 70.5 1.0 CG A:ASP1686 3.2 63.6 1.0 CD2 A:HIS1473 3.3 66.8 1.0 CD2 A:HIS1471 3.3 59.6 1.0 OD2 A:ASP1686 3.4 68.0 1.0 CD2 A:HIS1590 3.9 59.9 1.0 ND1 A:HIS1473 4.0 61.4 1.0 ND1 A:HIS1471 4.2 56.6 1.0 CE1 A:HIS1590 4.2 65.4 1.0 CG A:HIS1473 4.3 67.7 1.0 CG A:HIS1471 4.4 54.9 1.0 CB A:ASP1686 4.6 64.6 1.0 CD2 A:HIS1614 4.8 70.1 1.0 CA A:ASP1686 5.0 62.6 1.0 CG A:MET1503 5.0 53.1 1.0

J.H.Cheng, Y.H.Huang, J.J.Lin, C.Y.Huang. Crystal Structures of Monometallic Dihydropyrimidinase and the Human Dihydroorotase Domain K1556A Mutant Reveal No Lysine Carbamylation Within the Active Site Biochem. Biophys. Res. V. 505 439 2018COMMUN..
ISSN: ESSN 1090-2104
PubMed: 30268498
DOI: 10.1016/J.BBRC.2018.09.153