Zinc in PDB 2z2b: Deletion 107-116 Mutant of Dihydroorotase From E. Coli

All present enzymatic activity of Deletion 107-116 Mutant of Dihydroorotase From E. Coli:
3.5.2.3;

The structure of Deletion 107-116 Mutant of Dihydroorotase From E. Coli, PDB code: 2z2b 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)	40.00 / 1.85
Space group	P 32 1 2
Cell size a, b, c (Å), α, β, γ (°)	52.296, 52.296, 215.995, 90.00, 90.00, 120.00
R / Rfree (%)	19.1 / 24.5

The binding sites of Zinc atom in the Deletion 107-116 Mutant of Dihydroorotase From E. Coli (pdb code 2z2b). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Deletion 107-116 Mutant of Dihydroorotase From E. Coli, PDB code: 2z2b:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Deletion 107-116 Mutant of 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 Deletion 107-116 Mutant of Dihydroorotase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1337 b:41.5 occ:1.00 OQ2 A:KCX102 1.9 57.5 1.0 ND1 A:HIS129 2.0 58.0 1.0 NE2 A:HIS167 2.1 51.8 1.0 O A:HOH1346 2.3 41.0 1.0 CE1 A:HIS129 2.9 70.5 1.0 CX A:KCX102 2.9 62.5 1.0 CD2 A:HIS167 3.0 59.0 1.0 CE1 A:HIS167 3.1 59.4 1.0 CG A:HIS129 3.1 59.3 1.0 OQ1 A:KCX102 3.3 56.7 1.0 ZN A:ZN338 3.5 37.5 1.0 CB A:HIS129 3.6 61.3 1.0 NE2 A:HIS129 4.1 62.3 1.0 NZ A:KCX102 4.1 58.2 1.0 CE1 A:HIS16 4.1 54.8 1.0 ND1 A:HIS167 4.2 55.7 1.0 CG A:HIS167 4.2 55.1 1.0 CD2 A:HIS129 4.2 66.3 1.0 NE2 A:HIS16 4.3 52.6 1.0 CE2 A:TYR104 4.3 58.6 1.0 CA A:HIS129 4.4 54.3 1.0 OD2 A:ASP240 4.5 61.4 1.0 CE A:KCX102 4.6 58.6 1.0 O A:HOH1431 4.7 60.5 1.0 OD1 A:ASP240 4.9 55.1 1.0 CD2 A:TYR104 4.9 57.0 1.0

Zinc binding site 2 out of 2 in the Deletion 107-116 Mutant of 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 Deletion 107-116 Mutant of Dihydroorotase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn338 b:37.5 occ:1.00 O A:HOH1346 1.8 41.0 1.0 NE2 A:HIS18 2.0 53.9 1.0 OQ1 A:KCX102 2.2 56.7 1.0 NE2 A:HIS16 2.2 52.6 1.0 OD1 A:ASP240 2.2 55.1 1.0 CE1 A:HIS18 3.0 56.3 1.0 CX A:KCX102 3.1 62.5 1.0 CD2 A:HIS18 3.1 52.2 1.0 CD2 A:HIS16 3.1 54.5 1.0 CG A:ASP240 3.1 57.6 1.0 CE1 A:HIS16 3.2 54.8 1.0 OQ2 A:KCX102 3.4 57.5 1.0 ZN A:ZN1337 3.5 41.5 1.0 OD2 A:ASP240 3.5 61.4 1.0 ND1 A:HIS18 4.1 55.2 1.0 NZ A:KCX102 4.2 58.2 1.0 CG A:HIS18 4.2 50.3 1.0 CD2 A:HIS167 4.2 59.0 1.0 CG A:HIS16 4.3 50.8 1.0 ND1 A:HIS16 4.3 52.4 1.0 CB A:ASP240 4.3 55.1 1.0 CG A:MET42 4.4 54.4 1.0 NE2 A:HIS167 4.5 51.8 1.0 OH A:TYR104 4.7 56.3 1.0 CA A:ASP240 4.7 53.9 1.0

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