Zinc in PDB 4h00: The Crystal Structure of Mon-Zn Dihydropyrimidinase From Tetraodon Nigroviridis

The structure of The Crystal Structure of Mon-Zn Dihydropyrimidinase From Tetraodon Nigroviridis, PDB code: 4h00 was solved by Y.C.Hsieh, M.C.Chen, C.C.Hsu, S.I.Chan, Y.S.Yang, C.J.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.00
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	160.998, 160.998, 94.370, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 20.4

The binding sites of Zinc atom in the The Crystal Structure of Mon-Zn Dihydropyrimidinase From Tetraodon Nigroviridis (pdb code 4h00). 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 The Crystal Structure of Mon-Zn Dihydropyrimidinase From Tetraodon Nigroviridis, PDB code: 4h00:

Zinc binding site 1 out of 1 in the The Crystal Structure of Mon-Zn Dihydropyrimidinase From Tetraodon Nigroviridis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of Mon-Zn Dihydropyrimidinase From Tetraodon Nigroviridis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:37.9 occ:1.00 OD1 A:ASP322 2.1 25.7 1.0 OQ2 A:KCX155 2.2 39.9 1.0 NE2 A:HIS65 2.2 26.5 1.0 NE2 A:HIS63 2.2 22.3 1.0 CG A:ASP322 2.9 29.2 1.0 CD2 A:HIS63 3.1 21.4 1.0 CX A:KCX155 3.1 49.7 1.0 CD2 A:HIS65 3.1 22.7 1.0 CE1 A:HIS65 3.2 22.7 1.0 OD2 A:ASP322 3.2 32.5 1.0 OQ1 A:KCX155 3.3 50.8 1.0 CE1 A:HIS63 3.3 20.2 1.0 CB A:ASP322 4.1 24.8 1.0 CD2 A:HIS244 4.1 23.5 1.0 CG A:HIS63 4.3 23.7 1.0 CG A:HIS65 4.3 24.9 1.0 NZ A:KCX155 4.3 40.1 1.0 ND1 A:HIS65 4.3 25.1 1.0 ND1 A:HIS63 4.3 23.0 1.0 O A:HOH900 4.4 52.4 1.0 CA A:ASP322 4.5 24.6 1.0 NE2 A:HIS244 4.6 21.8 1.0 CE2 A:PHE97 4.6 19.7 1.0 CD2 A:PHE97 4.7 22.4 1.0 O A:HOH906 4.9 49.0 1.0 CE A:KCX155 4.9 32.3 1.0

Y.C.Hsieh, M.C.Chen, C.C.Hsu, S.I.Chan, Y.S.Yang, C.J.Chen. Lysine Carboxylation: Metal and Structural Requirements For Post-Translational Modification To Be Published.