Zinc in PDB 1xge: Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits

All present enzymatic activity of Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits:
3.5.2.3;

The structure of Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits, PDB code: 1xge was solved by M.Lee, C.W.Chan, J.M.Guss, R.I.Christopherson, M.J.Maher, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.582, 78.826, 180.222, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / 21.1

The binding sites of Zinc atom in the Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits (pdb code 1xge). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits, PDB code: 1xge:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:45.4 occ:1.00 OQ1 A:KCX102 1.9 39.7 1.0 NE2 A:HIS177 2.1 38.9 1.0 ND1 A:HIS139 2.1 38.3 1.0 O A:HOH1780 2.2 23.9 1.0 O4 A:DOR1410 2.7 51.9 1.0 CE1 A:HIS139 2.9 39.4 1.0 CX A:KCX102 2.9 41.4 1.0 CE1 A:HIS177 3.1 39.6 1.0 CD2 A:HIS177 3.1 39.7 1.0 CG A:HIS139 3.2 39.0 1.0 OQ2 A:KCX102 3.3 42.2 1.0 ZN A:ZN401 3.5 42.4 1.0 C4 A:DOR1410 3.6 52.1 1.0 CB A:HIS139 3.7 39.4 1.0 NE2 A:HIS139 4.1 38.8 1.0 CE1 A:HIS16 4.1 39.6 1.0 NZ A:KCX102 4.1 38.3 1.0 NE2 A:HIS16 4.2 39.3 1.0 ND1 A:HIS177 4.2 40.5 1.0 CD2 A:HIS139 4.2 39.5 1.0 CG A:HIS177 4.2 40.5 1.0 N3 A:DOR1410 4.3 50.8 1.0 CE2 A:TYR104 4.3 39.4 1.0 OD2 A:ASP250 4.4 39.3 1.0 C5 A:DOR1410 4.5 48.9 1.0 CE A:KCX102 4.6 38.5 1.0 CA A:HIS139 4.6 39.1 1.0 O A:LEU222 4.7 43.0 1.0 O A:HOH1421 4.7 41.6 1.0 CD2 A:TYR104 4.8 38.6 1.0 OD1 A:ASP250 4.9 38.9 1.0 CG A:ASP250 5.0 41.2 1.0

Zinc binding site 2 out of 4 in the Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:42.4 occ:1.00 O A:HOH1780 2.0 23.9 1.0 NE2 A:HIS18 2.0 37.3 1.0 NE2 A:HIS16 2.1 39.3 1.0 OD1 A:ASP250 2.2 38.9 1.0 OQ2 A:KCX102 2.3 42.2 1.0 CD2 A:HIS16 3.0 38.9 1.0 CD2 A:HIS18 3.0 38.4 1.0 CG A:ASP250 3.1 41.2 1.0 CE1 A:HIS18 3.1 38.1 1.0 CX A:KCX102 3.1 41.4 1.0 CE1 A:HIS16 3.2 39.6 1.0 OQ1 A:KCX102 3.5 39.7 1.0 OD2 A:ASP250 3.5 39.3 1.0 ZN A:ZN400 3.5 45.4 1.0 CG A:HIS18 4.1 37.1 1.0 CG A:HIS16 4.2 38.0 1.0 ND1 A:HIS18 4.2 36.3 1.0 NZ A:KCX102 4.2 38.3 1.0 ND1 A:HIS16 4.2 38.2 1.0 C5 A:DOR1410 4.2 48.9 1.0 CD2 A:HIS177 4.2 39.7 1.0 CB A:ASP250 4.3 39.8 1.0 C4 A:DOR1410 4.3 52.1 1.0 C6 A:DOR1410 4.4 47.0 1.0 O4 A:DOR1410 4.4 51.9 1.0 CG A:MET42 4.4 38.5 1.0 NE2 A:HIS177 4.4 38.9 1.0 OH A:TYR104 4.6 37.8 1.0 CA A:ASP250 4.7 39.7 1.0 N3 A:DOR1410 4.9 50.8 1.0

Zinc binding site 3 out of 4 in the Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn400 b:43.8 occ:1.00 OQ1 B:KCX102 2.0 39.1 1.0 NE2 B:HIS177 2.1 38.9 1.0 ND1 B:HIS139 2.1 38.4 1.0 O5 B:NCD2410 2.2 44.6 1.0 O4 B:NCD2410 2.6 41.6 1.0 C4 B:NCD2410 2.7 43.6 1.0 CE1 B:HIS139 3.0 39.0 1.0 CE1 B:HIS177 3.0 38.8 1.0 CX B:KCX102 3.0 39.0 1.0 CD2 B:HIS177 3.1 38.1 1.0 CG B:HIS139 3.2 39.6 1.0 OQ2 B:KCX102 3.4 38.5 1.0 CB B:HIS139 3.7 39.1 1.0 ZN B:ZN401 3.9 42.9 1.0 ND1 B:HIS177 4.1 37.8 1.0 NZ B:KCX102 4.1 36.4 1.0 NE2 B:HIS139 4.2 38.3 1.0 C5 B:NCD2410 4.2 41.4 1.0 CG B:HIS177 4.2 38.6 1.0 CD2 B:HIS139 4.3 39.6 1.0 CE1 B:HIS16 4.3 41.4 1.0 CE2 B:TYR104 4.4 40.6 1.0 NE2 B:HIS16 4.5 39.8 1.0 CA B:HIS139 4.5 39.1 1.0 CE B:KCX102 4.6 38.6 1.0 OG1 B:THR109 4.6 49.5 1.0 N3 B:NCD2410 4.6 42.1 1.0 CG2 B:THR109 4.7 48.0 1.0 OD2 B:ASP250 4.7 40.1 1.0 CB B:THR109 4.9 48.5 1.0 O B:LEU222 4.9 41.0 1.0 CD2 B:TYR104 5.0 38.9 1.0

Zinc binding site 4 out of 4 in the Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:42.9 occ:1.00 NE2 B:HIS18 2.0 37.8 1.0 O4 B:NCD2410 2.0 41.6 1.0 OQ2 B:KCX102 2.1 38.5 1.0 OD1 B:ASP250 2.1 38.0 1.0 NE2 B:HIS16 2.2 39.8 1.0 CD2 B:HIS18 2.9 38.2 1.0 CE1 B:HIS18 3.0 38.9 1.0 CD2 B:HIS16 3.0 38.7 1.0 CG B:ASP250 3.0 38.8 1.0 CX B:KCX102 3.1 39.0 1.0 C4 B:NCD2410 3.1 43.6 1.0 CE1 B:HIS16 3.2 41.4 1.0 OD2 B:ASP250 3.5 40.1 1.0 OQ1 B:KCX102 3.6 39.1 1.0 C5 B:NCD2410 3.8 41.4 1.0 ZN B:ZN400 3.9 43.8 1.0 C6 B:NCD2410 4.0 41.4 1.0 CG B:HIS18 4.1 38.1 1.0 ND1 B:HIS18 4.1 37.7 1.0 O5 B:NCD2410 4.1 44.6 1.0 NZ B:KCX102 4.1 36.4 1.0 CG B:HIS16 4.2 39.1 1.0 CB B:ASP250 4.3 38.1 1.0 ND1 B:HIS16 4.3 40.7 1.0 CD2 B:HIS177 4.3 38.1 1.0 CG B:MET42 4.3 38.1 1.0 NE2 B:HIS177 4.5 38.9 1.0 N3 B:NCD2410 4.6 42.1 1.0 OH B:TYR104 4.6 39.1 1.0 CA B:ASP250 4.7 37.6 1.0 O61 B:NCD2410 4.7 41.9 1.0 C61 B:NCD2410 4.9 41.6 1.0 CB B:MET42 5.0 38.0 1.0

M.Lee, C.W.Chan, J.M.Guss, R.I.Christopherson, M.J.Maher. Dihydroorotase From Escherichia Coli: Loop Movement and Cooperativity Between Subunits J.Mol.Biol. V. 348 523 2005.
ISSN: ISSN 0022-2836
PubMed: 15826651
DOI: 10.1016/J.JMB.2005.01.067