Zinc in PDB 4h01: The Crystal Structure of Di-Zn Dihydropyrimidinase From Tetraodon Nigroviridis

The structure of The Crystal Structure of Di-Zn Dihydropyrimidinase From Tetraodon Nigroviridis, PDB code: 4h01 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 (°)	160.478, 160.478, 93.296, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 21.1

The binding sites of Zinc atom in the The Crystal Structure of Di-Zn Dihydropyrimidinase From Tetraodon Nigroviridis (pdb code 4h01). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Crystal Structure of Di-Zn Dihydropyrimidinase From Tetraodon Nigroviridis, PDB code: 4h01:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Crystal Structure of Di-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 Di-Zn Dihydropyrimidinase From Tetraodon Nigroviridis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:17.2 occ:1.00 OQ1 A:KCX155 2.0 17.4 1.0 NE2 A:HIS63 2.0 14.2 1.0 O A:HOH915 2.0 22.6 1.0 NE2 A:HIS65 2.0 17.2 1.0 OD1 A:ASP322 2.2 14.6 1.0 CD2 A:HIS63 3.0 13.0 1.0 CE1 A:HIS63 3.0 13.7 1.0 CD2 A:HIS65 3.0 13.9 1.0 CE1 A:HIS65 3.0 14.5 1.0 CX A:KCX155 3.1 15.5 1.0 CG A:ASP322 3.2 17.6 1.0 OQ2 A:KCX155 3.7 15.2 1.0 OD2 A:ASP322 3.7 17.9 1.0 ZN A:ZN602 3.7 20.0 1.0 CD2 A:HIS244 4.0 10.9 1.0 NZ A:KCX155 4.1 13.9 1.0 ND1 A:HIS63 4.1 12.2 1.0 CG A:HIS63 4.2 12.6 1.0 ND1 A:HIS65 4.2 13.4 1.0 CG A:HIS65 4.2 14.2 1.0 O A:HOH916 4.2 30.0 1.0 CB A:ASP322 4.3 13.9 1.0 NE2 A:HIS244 4.4 10.7 1.0 CE2 A:PHE97 4.6 12.0 1.0 CA A:ASP322 4.6 13.8 1.0 CD2 A:PHE97 4.6 12.3 1.0

Zinc binding site 2 out of 2 in the The Crystal Structure of Di-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 2 of The Crystal Structure of Di-Zn Dihydropyrimidinase From Tetraodon Nigroviridis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn602 b:20.0 occ:1.00 OQ2 A:KCX155 2.0 15.2 1.0 NE2 A:HIS244 2.1 10.7 1.0 ND1 A:HIS188 2.2 13.0 1.0 O A:HOH915 2.4 22.6 1.0 CE1 A:HIS188 2.9 13.9 1.0 CD2 A:HIS244 3.0 10.9 1.0 CX A:KCX155 3.0 15.5 1.0 CE1 A:HIS244 3.1 11.7 1.0 OQ1 A:KCX155 3.3 17.4 1.0 CG A:HIS188 3.3 13.2 1.0 CB A:HIS188 3.7 12.8 1.0 ZN A:ZN601 3.7 17.2 1.0 O A:GLY294 3.9 19.5 1.0 NE2 A:HIS188 4.1 13.8 1.0 CE1 A:PHE157 4.1 17.1 1.0 NZ A:KCX155 4.1 13.9 1.0 CG A:HIS244 4.2 11.1 1.0 ND1 A:HIS244 4.2 11.0 1.0 CD2 A:HIS188 4.3 14.1 1.0 CG2 A:VAL243 4.4 10.4 1.0 OH A:TYR160 4.4 23.6 1.0 CE A:KCX155 4.5 15.5 1.0 CA A:HIS188 4.6 12.3 1.0 O A:HOH916 4.7 30.0 1.0 CD1 A:PHE157 4.7 14.2 1.0 CE1 A:HIS63 4.8 13.7 1.0 NE2 A:HIS63 4.8 14.2 1.0 CE2 A:TYR160 4.8 22.7 1.0 C A:GLY294 4.9 17.1 1.0 CD A:PRO295 5.0 15.9 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.