Zinc in PDB 1q0a: Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222)

The structure of Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222), PDB code: 1q0a was solved by A.Changela, K.Chen, Y.Xue, J.Holschen, C.E.Outten, T.V.O'halloran, A.Mondragon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.59 / 2.00
Space group	C 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	84.666, 170.707, 42.208, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 25.8

The binding sites of Zinc atom in the Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222) (pdb code 1q0a). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222), PDB code: 1q0a:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in the Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:15.5 occ:1.00 O2 A:SO4301 2.1 16.9 1.0 SG A:CYS124 2.4 14.9 1.0 SG A:CYS114 2.4 15.8 1.0 S A:SO4301 3.2 19.8 1.0 CB A:CYS124 3.3 13.5 1.0 CB A:CYS114 3.4 15.6 1.0 O3 A:SO4301 3.4 16.0 1.0 CA A:CYS124 3.5 13.7 1.0 ZN A:ZN402 3.6 16.9 1.0 O4 A:SO4301 3.7 20.6 1.0 N A:SER125 3.8 12.5 1.0 CA A:CYS114 3.9 16.7 1.0 C A:CYS124 4.1 13.1 1.0 OG A:SER125 4.2 14.9 1.0 N A:CYS115 4.3 16.6 1.0 O1 A:SO4301 4.4 18.0 1.0 C A:CYS114 4.5 17.7 1.0 N A:ILE126 4.6 12.2 1.0 N A:CYS124 4.6 12.8 1.0 CG1 A:ILE126 4.7 14.1 1.0 CD1 A:ILE126 4.7 16.0 1.0 N A:GLY116 4.9 15.9 1.0 CA A:SER125 4.9 12.6 1.0

Zinc binding site 2 out of 5 in the Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:16.9 occ:1.00 O3 A:SO4301 2.2 16.0 1.0 ND1 A:HIS119 2.2 14.6 1.0 SG A:CYS115 2.3 14.0 1.0 O4 A:SO4301 3.0 20.6 1.0 S A:SO4301 3.0 19.8 1.0 CG A:HIS119 3.1 14.6 1.0 CB A:HIS119 3.2 16.1 1.0 CE1 A:HIS119 3.3 13.4 1.0 CB A:CYS115 3.3 15.8 1.0 ZN A:ZN401 3.6 15.5 1.0 O2 A:SO4301 3.7 16.9 1.0 N A:CYS115 3.7 16.6 1.0 CA A:CYS115 4.1 16.2 1.0 CD2 A:HIS119 4.3 12.2 1.0 O1 A:SO4301 4.3 18.0 1.0 NE2 A:HIS119 4.4 12.9 1.0 N A:GLY116 4.4 15.9 1.0 CB B:CYS115 4.5 16.2 1.0 CA A:HIS119 4.6 17.1 1.0 C A:CYS115 4.7 16.7 1.0 SG A:CYS114 4.7 15.8 1.0 C A:CYS114 4.9 17.7 1.0 O3 B:SO4302 5.0 16.4 1.0 CE1 B:HIS119 5.0 16.6 1.0

Zinc binding site 3 out of 5 in the Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn405 b:20.6 occ:1.00 NE2 A:HIS53 2.1 16.0 1.0 CD2 A:HIS53 3.1 18.2 1.0 CE1 A:HIS53 3.1 17.9 1.0 O A:HOH421 4.2 21.7 1.0 ND1 A:HIS53 4.2 13.7 1.0 CG A:HIS53 4.2 17.6 1.0 CD A:LYS49 4.9 33.9 1.0

Zinc binding site 4 out of 5 in the Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn403 b:19.1 occ:1.00 O1 B:SO4302 2.1 19.9 1.0 SG B:CYS114 2.4 18.7 1.0 SG B:CYS124 2.4 18.9 1.0 S B:SO4302 3.2 20.3 1.0 CB B:CYS114 3.3 19.2 1.0 CB B:CYS124 3.3 16.7 1.0 O3 B:SO4302 3.4 16.4 1.0 CA B:CYS124 3.5 16.9 1.0 ZN B:ZN404 3.7 18.1 1.0 O2 B:SO4302 3.7 21.7 1.0 N B:SER125 3.8 16.6 1.0 CA B:CYS114 3.8 17.9 1.0 C B:CYS124 4.1 16.0 1.0 OG B:SER125 4.3 16.8 1.0 N B:CYS115 4.3 17.8 1.0 O4 B:SO4302 4.4 19.3 1.0 C B:CYS114 4.5 17.8 1.0 N B:CYS124 4.6 19.1 1.0 N B:ILE126 4.6 19.4 1.0 CG1 B:ILE126 4.6 18.2 1.0 CD1 B:ILE126 4.7 15.7 1.0 N B:GLY116 4.9 17.5 1.0 CA B:SER125 4.9 18.4 1.0

Zinc binding site 5 out of 5 in the Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of the Zn(II) Form of E. Coli Zntr, A Zinc-Sensing Transcriptional Regulator (Space Group C222) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn404 b:18.1 occ:1.00 O3 B:SO4302 2.2 16.4 1.0 SG B:CYS115 2.2 15.2 1.0 ND1 B:HIS119 2.3 16.0 1.0 O2 B:SO4302 3.0 21.7 1.0 CG B:HIS119 3.1 16.3 1.0 S B:SO4302 3.1 20.3 1.0 CB B:HIS119 3.1 17.7 1.0 CB B:CYS115 3.3 16.2 1.0 CE1 B:HIS119 3.4 16.6 1.0 ZN B:ZN403 3.7 19.1 1.0 N B:CYS115 3.7 17.8 1.0 O1 B:SO4302 3.8 19.9 1.0 CA B:CYS115 4.1 16.1 1.0 CD2 B:HIS119 4.3 12.9 1.0 O4 B:SO4302 4.3 19.3 1.0 CB A:CYS115 4.4 15.8 1.0 NE2 B:HIS119 4.4 15.9 1.0 N B:GLY116 4.5 17.5 1.0 CA B:HIS119 4.6 18.6 1.0 SG B:CYS114 4.6 18.7 1.0 C B:CYS115 4.7 17.3 1.0 OG1 B:THR117 4.8 16.5 1.0 C B:CYS114 4.9 17.8 1.0 CE1 A:HIS119 4.9 13.4 1.0 O B:HIS119 4.9 17.8 1.0 ND1 A:HIS119 5.0 14.6 1.0

A.Changela, K.Chen, Y.Xue, J.Holschen, C.E.Outten, T.V.O'halloran, A.Mondragon. Molecular Basis of Metal-Ion Selectivity and Zeptomolar Sensitivity By Cuer Science V. 301 1383 2003.
ISSN: ISSN 0036-8075
PubMed: 12958362
DOI: 10.1126/SCIENCE.1085950