Zinc in PDB 6hfj: Human Dihydroorotase Mutant F1563A Co-Crystallized with Carbamoyl Aspartate at pH 7.5

All present enzymatic activity of Human Dihydroorotase Mutant F1563A Co-Crystallized with Carbamoyl Aspartate at pH 7.5:
2.1.3.2; 3.5.2.3; 6.3.5.5;

The structure of Human Dihydroorotase Mutant F1563A Co-Crystallized with Carbamoyl Aspartate at pH 7.5, PDB code: 6hfj was solved by S.Ramon-Maiques, A.Grande Garcia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.92 / 1.20
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	81.932, 158.887, 60.923, 90.00, 90.00, 90.00
R / Rfree (%)	12.8 / 14.8

The binding sites of Zinc atom in the Human Dihydroorotase Mutant F1563A Co-Crystallized with Carbamoyl Aspartate at pH 7.5 (pdb code 6hfj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Human Dihydroorotase Mutant F1563A Co-Crystallized with Carbamoyl Aspartate at pH 7.5, PDB code: 6hfj:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Human Dihydroorotase Mutant F1563A Co-Crystallized with Carbamoyl Aspartate at pH 7.5


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Dihydroorotase Mutant F1563A Co-Crystallized with Carbamoyl Aspartate at pH 7.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1901 b:11.7 occ:0.75 OQ1 A:KCX1556 1.9 13.7 1.0 O A:HOH2129 2.0 14.3 1.0 NE2 A:HIS1614 2.0 13.2 1.0 ND1 A:HIS1590 2.1 13.6 1.0 CX A:KCX1556 2.9 14.0 1.0 CE1 A:HIS1590 2.9 14.2 1.0 HB2 A:HIS1590 3.0 15.5 1.0 CE1 A:HIS1614 3.0 12.9 1.0 CD2 A:HIS1614 3.1 13.1 1.0 HE1 A:HIS1590 3.1 17.1 1.0 O4 A:DOR1908 3.1 23.2 0.7 CG A:HIS1590 3.1 13.2 1.0 HE1 A:HIS1614 3.2 15.5 1.0 HE1 A:HIS1471 3.2 15.8 1.0 OQ2 A:KCX1556 3.2 14.7 1.0 HD2 A:HIS1614 3.3 15.7 1.0 ZN A:ZN1902 3.3 12.5 0.9 CB A:HIS1590 3.5 12.9 1.0 HE2 A:TYR1558 3.6 23.8 0.4 C4 A:DOR1908 3.7 20.5 0.7 H52 A:DOR1908 3.8 26.2 0.7 CE1 A:HIS1471 3.9 13.1 1.0 HE1 A:TYR1558 4.0 17.4 0.6 NE2 A:HIS1471 4.0 12.1 1.0 CE2 A:TYR1558 4.0 19.8 0.4 OD2 A:ASP1686 4.1 14.5 1.0 NE2 A:HIS1590 4.1 14.8 1.0 ND1 A:HIS1614 4.1 12.7 1.0 NZ A:KCX1556 4.1 15.4 1.0 CD2 A:HIS1590 4.2 13.8 1.0 CG A:HIS1614 4.2 12.7 1.0 HD3 A:PRO1662 4.2 18.0 1.0 HA A:HIS1590 4.2 13.2 1.0 HB3 A:HIS1590 4.2 15.5 1.0 HE2 A:KCX1556 4.3 17.4 1.0 HN3 A:DOR1908 4.3 26.9 0.7 N3 A:DOR1908 4.3 22.4 0.7 C5 A:DOR1908 4.3 21.8 0.7 OH A:TYR1558 4.5 21.9 0.4 HB3 A:CYS1613 4.5 15.4 1.0 CA A:HIS1590 4.5 10.9 1.0 CZ A:TYR1558 4.5 20.1 0.4 O A:ARG1661 4.5 16.9 1.0 HB2 A:CYS1613 4.5 15.4 1.0 CE A:KCX1556 4.6 14.5 1.0 CE1 A:TYR1558 4.6 14.5 0.6 OD1 A:ASP1686 4.6 14.0 1.0 CG A:ASP1686 4.6 14.3 1.0 HE3 A:KCX1556 4.7 17.4 1.0 HD1 A:TYR1558 4.7 17.6 0.6 CD2 A:TYR1558 4.7 18.9 0.4 HD2 A:TYR1558 4.8 22.7 0.4 HE2 A:HIS1590 4.8 17.8 1.0 HZ A:KCX1556 4.8 18.5 1.0 HD1 A:HIS1614 4.9 15.2 1.0 CB A:CYS1613 5.0 12.8 1.0 H51 A:DOR1908 5.0 26.2 0.7

Zinc binding site 2 out of 4 in the Human Dihydroorotase Mutant F1563A Co-Crystallized with Carbamoyl Aspartate at pH 7.5


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Dihydroorotase Mutant F1563A Co-Crystallized with Carbamoyl Aspartate at pH 7.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1902 b:12.5 occ:0.88 O A:HOH2129 1.9 14.3 1.0 NE2 A:HIS1471 2.0 12.1 1.0 NE2 A:HIS1473 2.0 13.3 1.0 OQ2 A:KCX1556 2.2 14.7 1.0 OD1 A:ASP1686 2.2 14.0 1.0 H52 A:DOR1908 2.9 26.2 0.7 CD2 A:HIS1471 3.0 11.8 1.0 CE1 A:HIS1473 3.0 12.3 1.0 CX A:KCX1556 3.0 14.0 1.0 CE1 A:HIS1471 3.0 13.1 1.0 CD2 A:HIS1473 3.1 13.5 1.0 CG A:ASP1686 3.1 14.3 1.0 HD2 A:HIS1471 3.1 14.2 1.0 HE1 A:HIS1473 3.2 14.8 1.0 HE1 A:HIS1471 3.2 15.8 1.0 HD2 A:HIS1473 3.3 16.2 1.0 ZN A:ZN1901 3.3 11.7 0.8 OQ1 A:KCX1556 3.4 13.7 1.0 HG3 A:MET1503 3.4 18.1 1.0 OD2 A:ASP1686 3.4 14.5 1.0 H6 A:DOR1908 3.5 25.3 0.7 C5 A:DOR1908 3.8 21.8 0.7 HD2 A:HIS1614 3.9 15.7 1.0 HH A:TYR1558 4.0 15.3 0.6 ND1 A:HIS1471 4.1 14.2 1.0 ND1 A:HIS1473 4.1 14.0 1.0 CG A:HIS1471 4.1 11.8 1.0 HA A:ASP1686 4.1 15.2 1.0 NZ A:KCX1556 4.2 15.4 1.0 C6 A:DOR1908 4.2 21.1 0.7 CG A:HIS1473 4.2 13.7 1.0 C4 A:DOR1908 4.2 20.5 0.7 HE1 A:TYR1558 4.3 17.4 0.6 HZ A:KCX1556 4.3 18.5 1.0 CB A:ASP1686 4.4 13.6 1.0 CG A:MET1503 4.4 15.1 1.0 NE2 A:HIS1614 4.4 13.2 1.0 CD2 A:HIS1614 4.5 13.1 1.0 O4 A:DOR1908 4.5 23.2 0.7 HE3 A:MET1503 4.5 19.0 1.0 HB2 A:ASP1686 4.5 16.3 1.0 H51 A:DOR1908 4.6 26.2 0.7 CA A:ASP1686 4.8 12.7 1.0 OH A:TYR1558 4.8 12.7 0.6 HB2 A:ALA1688 4.8 18.5 1.0 HG2 A:MET1503 4.8 18.1 1.0 HE2 A:TYR1558 4.8 23.8 0.4 HD1 A:HIS1473 4.9 16.8 1.0 HB2 A:MET1503 4.9 16.6 1.0 N3 A:DOR1908 4.9 22.4 0.7

Zinc binding site 3 out of 4 in the Human Dihydroorotase Mutant F1563A Co-Crystallized with Carbamoyl Aspartate at pH 7.5


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Human Dihydroorotase Mutant F1563A Co-Crystallized with Carbamoyl Aspartate at pH 7.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1903 b:12.3 occ:0.50 ND1 A:HIS1471 2.0 14.2 1.0 O A:HOH2159 2.0 14.2 1.0 OE1 A:GLU1637 2.1 14.9 1.0 SG A:CYS1613 2.3 13.9 1.0 HB3 A:CYS1613 2.7 15.4 1.0 HB2 A:HIS1471 2.8 14.7 1.0 CD A:GLU1637 2.9 13.1 1.0 CE1 A:HIS1471 2.9 13.1 1.0 CB A:CYS1613 3.0 12.8 1.0 OE2 A:GLU1637 3.0 14.1 1.0 CG A:HIS1471 3.1 11.8 1.0 HE1 A:HIS1471 3.1 15.8 1.0 HE3 A:MET1503 3.2 19.0 1.0 HA A:CYS1613 3.2 14.2 1.0 CB A:HIS1471 3.4 12.2 1.0 HE1 A:MET1503 3.6 19.0 1.0 CA A:CYS1613 3.6 11.9 1.0 CE A:MET1503 3.7 15.8 1.0 HB2 A:CYS1613 3.8 15.4 1.0 HE2 A:MET1503 3.9 19.0 1.0 HB3 A:HIS1471 4.0 14.7 1.0 H A:HIS1614 4.1 14.6 1.0 NE2 A:HIS1471 4.1 12.1 1.0 CD2 A:HIS1471 4.1 11.8 1.0 HG21 A:VAL1588 4.1 18.0 1.0 HD2 A:HIS1611 4.2 15.5 1.0 HB A:VAL1588 4.2 16.8 1.0 CG A:GLU1637 4.2 12.8 1.0 HG23 A:VAL1470 4.3 16.1 1.0 HG2 A:GLU1637 4.4 15.3 1.0 HE2 A:HIS1611 4.4 16.3 1.0 O A:VAL1470 4.4 12.9 1.0 HA A:HIS1471 4.4 13.2 1.0 HG3 A:GLU1637 4.5 15.3 1.0 CA A:HIS1471 4.6 11.0 1.0 O A:HOH2284 4.6 20.1 1.0 N A:CYS1613 4.6 11.4 1.0 N A:HIS1614 4.6 12.2 1.0 C A:CYS1613 4.7 12.8 1.0 HG23 A:VAL1588 4.7 18.0 1.0 CG2 A:VAL1588 4.8 15.0 1.0 H A:CYS1613 4.8 13.7 1.0 CD2 A:HIS1611 4.8 12.9 1.0 HB3 A:ALA1684 4.8 17.5 1.0 HE2 A:KCX1556 4.8 17.4 1.0 HG11 A:VAL1588 4.8 17.0 1.0 CB A:VAL1588 4.9 14.0 1.0 NE2 A:HIS1611 4.9 13.6 1.0 HD2 A:HIS1471 5.0 14.2 1.0 HD2 A:KCX1556 5.0 17.4 1.0

Zinc binding site 4 out of 4 in the Human Dihydroorotase Mutant F1563A Co-Crystallized with Carbamoyl Aspartate at pH 7.5


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Human Dihydroorotase Mutant F1563A Co-Crystallized with Carbamoyl Aspartate at pH 7.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1904 b:22.3 occ:1.00 HE2 A:HIS1734 1.3 19.6 1.0 O A:HOH2312 1.8 22.3 1.0 NE2 A:HIS1734 2.1 16.3 1.0 O A:HOH2318 2.1 16.0 1.0 CE1 A:HIS1734 2.8 16.8 1.0 HE1 A:HIS1734 2.9 20.1 1.0 CD2 A:HIS1734 3.2 15.5 1.0 HD2 A:HIS1734 3.6 18.6 1.0 ND1 A:HIS1734 4.0 14.4 1.0 HD2 A:HIS1733 4.1 17.1 1.0 CG A:HIS1734 4.3 13.6 1.0 O A:HOH2350 4.4 33.5 1.0 HG3 A:PRO1465 4.5 24.4 1.0 HB3 A:LEU1729 4.6 20.5 1.0 HD13 A:LEU1729 4.7 24.9 1.0 HD1 A:HIS1734 4.8 17.2 1.0 CD2 A:HIS1733 4.8 14.2 1.0 O A:HOH2139 4.9 29.3 1.0

F.Del Cano-Ochoa, A.Grande-Garcia, M.Reverte-Lopez, M.D'abramo, S.Ramon-Maiques. Characterization of the Catalytic Flexible Loop in the Dihydroorotase Domain of the Human Multi-Enzymatic Protein Cad. J. Biol. Chem. V. 293 18903 2018.
ISSN: ESSN 1083-351X
PubMed: 30315107
DOI: 10.1074/JBC.RA118.005494