Zinc in PDB 2z26: THR110ALA Dihydroorotase From E. Coli

All present enzymatic activity of THR110ALA Dihydroorotase From E. Coli:
3.5.2.3;

The structure of THR110ALA Dihydroorotase From E. Coli, PDB code: 2z26 was solved by M.Lee, M.J.Maher, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.00 / 1.29
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.493, 78.885, 180.091, 90.00, 90.00, 90.00
R / Rfree (%)	12.9 / 15.4

The binding sites of Zinc atom in the THR110ALA Dihydroorotase From E. Coli (pdb code 2z26). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the THR110ALA Dihydroorotase From E. Coli, PDB code: 2z26:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the THR110ALA Dihydroorotase From E. Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of THR110ALA Dihydroorotase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:14.3 occ:1.00 OQ2 A:KCX102 1.9 12.0 1.0 NE2 A:HIS177 2.0 12.9 1.0 ND1 A:HIS139 2.1 13.9 1.0 O A:HOH1441 2.1 14.1 1.0 CE1 A:HIS139 2.9 14.9 1.0 O4 A:DOR1410 2.9 21.7 1.0 CX A:KCX102 2.9 12.7 1.0 CE1 A:HIS177 3.0 12.4 1.0 CD2 A:HIS177 3.1 13.8 1.0 CG A:HIS139 3.2 12.6 1.0 OQ1 A:KCX102 3.3 11.7 1.0 ZN A:ZN401 3.5 12.4 1.0 C4 A:DOR1410 3.6 16.8 1.0 CB A:HIS139 3.6 13.0 1.0 NE2 A:HIS139 4.0 14.0 1.0 CE1 A:HIS16 4.0 13.0 1.0 NZ A:KCX102 4.1 11.2 1.0 ND1 A:HIS177 4.1 12.0 1.0 N3 A:DOR1410 4.2 18.0 1.0 CD2 A:HIS139 4.2 14.2 1.0 NE2 A:HIS16 4.2 11.4 1.0 CG A:HIS177 4.2 12.1 1.0 OD2 A:ASP250 4.4 13.7 1.0 CE2 A:TYR104 4.4 12.9 1.0 O A:LEU222 4.4 17.8 1.0 C5 A:DOR1410 4.5 17.5 1.0 CE A:KCX102 4.6 11.9 1.0 CA A:HIS139 4.6 13.1 1.0 O A:HOH1779 4.7 38.5 1.0 OD1 A:ASP250 4.7 11.5 1.0 CG A:ASP250 4.9 12.1 1.0 CD2 A:TYR104 4.9 13.2 1.0

Zinc binding site 2 out of 4 in the THR110ALA Dihydroorotase From E. Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of THR110ALA Dihydroorotase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:12.4 occ:1.00 O A:HOH1441 2.0 14.1 1.0 NE2 A:HIS18 2.1 10.8 1.0 NE2 A:HIS16 2.1 11.4 1.0 OD1 A:ASP250 2.1 11.5 1.0 OQ1 A:KCX102 2.2 11.7 1.0 CX A:KCX102 3.0 12.7 1.0 CD2 A:HIS16 3.0 10.9 1.0 CE1 A:HIS18 3.1 11.8 1.0 CD2 A:HIS18 3.1 11.1 1.0 CG A:ASP250 3.1 12.1 1.0 CE1 A:HIS16 3.1 13.0 1.0 OQ2 A:KCX102 3.4 12.0 1.0 ZN A:ZN400 3.5 14.3 1.0 OD2 A:ASP250 3.5 13.7 1.0 NZ A:KCX102 4.1 11.2 1.0 ND1 A:HIS18 4.2 11.0 1.0 ND1 A:HIS16 4.2 11.6 1.0 CG A:HIS16 4.2 10.6 1.0 CG A:HIS18 4.2 11.0 1.0 CD2 A:HIS177 4.3 13.8 1.0 C5 A:DOR1410 4.3 17.5 1.0 CB A:ASP250 4.3 11.6 1.0 NE2 A:HIS177 4.3 12.9 1.0 C6 A:DOR1410 4.3 15.4 1.0 C4 A:DOR1410 4.3 16.8 1.0 CG A:MET42 4.4 11.9 1.0 O4 A:DOR1410 4.5 21.7 1.0 OH A:TYR104 4.6 12.7 1.0 CA A:ASP250 4.7 10.8 1.0 N3 A:DOR1410 4.7 18.0 1.0

Zinc binding site 3 out of 4 in the THR110ALA Dihydroorotase From E. Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of THR110ALA Dihydroorotase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn400 b:17.9 occ:1.00 OQ2 B:KCX102 1.9 15.4 1.0 O5 B:NCD1420 1.9 15.7 0.5 NE2 B:HIS177 2.0 16.3 1.0 ND1 B:HIS139 2.1 17.0 1.0 O B:HOH1431 2.1 14.5 0.5 O4 B:NCD1420 2.5 14.6 0.5 C4 B:NCD1420 2.5 15.6 0.5 CE1 B:HIS139 2.9 18.9 1.0 CX B:KCX102 2.9 15.4 1.0 O4 B:DOR1430 2.9 18.4 0.5 CE1 B:HIS177 3.0 14.4 1.0 CD2 B:HIS177 3.1 14.3 1.0 CG B:HIS139 3.2 16.0 1.0 OQ1 B:KCX102 3.3 15.3 1.0 ZN B:ZN401 3.6 15.5 1.0 CB B:HIS139 3.6 16.9 1.0 C4 B:DOR1430 3.7 18.5 0.5 C5 B:NCD1420 4.0 15.2 0.5 NE2 B:HIS139 4.0 20.0 1.0 NZ B:KCX102 4.1 16.7 1.0 ND1 B:HIS177 4.1 13.4 1.0 CE1 B:HIS16 4.2 14.0 1.0 CD2 B:HIS139 4.2 18.4 1.0 CG B:HIS177 4.2 13.3 1.0 N3 B:DOR1430 4.2 16.3 0.5 CE2 B:TYR104 4.3 17.3 1.0 NE2 B:HIS16 4.4 14.3 1.0 OD2 B:ASP250 4.5 16.4 1.0 N3 B:NCD1420 4.6 19.0 0.5 CA B:HIS139 4.6 16.2 1.0 O B:LEU222 4.6 23.9 1.0 CE B:KCX102 4.6 17.1 1.0 C5 B:DOR1430 4.7 16.9 0.5 CD2 B:TYR104 4.8 16.3 1.0 OD1 B:ASP250 4.9 14.4 1.0

Zinc binding site 4 out of 4 in the THR110ALA Dihydroorotase From E. Coli


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of THR110ALA Dihydroorotase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:15.5 occ:1.00 O4 B:NCD1420 1.9 14.6 0.5 O B:HOH1431 2.0 14.5 0.5 NE2 B:HIS18 2.1 13.6 1.0 NE2 B:HIS16 2.1 14.3 1.0 OD1 B:ASP250 2.1 14.4 1.0 OQ1 B:KCX102 2.2 15.3 1.0 C4 B:NCD1420 3.0 15.6 0.5 CD2 B:HIS18 3.0 14.1 1.0 CE1 B:HIS18 3.0 15.3 1.0 CX B:KCX102 3.1 15.4 1.0 CD2 B:HIS16 3.1 14.8 1.0 CG B:ASP250 3.1 14.8 1.0 CE1 B:HIS16 3.1 14.0 1.0 OQ2 B:KCX102 3.5 15.4 1.0 OD2 B:ASP250 3.5 16.4 1.0 ZN B:ZN400 3.6 17.9 1.0 C5 B:NCD1420 3.7 15.2 0.5 O5 B:NCD1420 3.8 15.7 0.5 C6 B:NCD1420 4.0 16.4 0.5 NZ B:KCX102 4.1 16.7 1.0 ND1 B:HIS18 4.2 13.7 1.0 CG B:HIS18 4.2 13.8 1.0 ND1 B:HIS16 4.2 14.1 1.0 CD2 B:HIS177 4.2 14.3 1.0 CG B:HIS16 4.2 13.5 1.0 CB B:ASP250 4.3 13.2 1.0 NE2 B:HIS177 4.3 16.3 1.0 C4 B:DOR1430 4.4 18.5 0.5 CG B:MET42 4.4 15.8 1.0 C6 B:DOR1430 4.5 16.3 0.5 C5 B:DOR1430 4.5 16.9 0.5 O4 B:DOR1430 4.5 18.4 0.5 N3 B:NCD1420 4.5 19.0 0.5 OH B:TYR104 4.6 17.4 1.0 O61 B:NCD1420 4.6 18.1 0.5 CA B:ASP250 4.7 12.5 1.0 N3 B:DOR1430 4.7 16.3 0.5 C61 B:NCD1420 4.8 17.7 0.5

M.Lee, M.J.Maher, R.I.Christopherson, J.M.Guss. Kinetic and Structural Analysis of Mutant Escherichia Coli Dihydroorotases: A Flexible Loop Stabilizes the Transition State Biochemistry V. 46 10538 2007.
ISSN: ISSN 0006-2960
PubMed: 17711307
DOI: 10.1021/BI701098E