Zinc in PDB 4ntn: E.Coli Qued, Semet Protein, 2A Resolution

All present enzymatic activity of E.Coli Qued, Semet Protein, 2A Resolution:
4.1.2.50;

The structure of E.Coli Qued, Semet Protein, 2A Resolution, PDB code: 4ntn was solved by V.Bandarian, S.A.Roberts, Z.D.Miles, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.80 / 1.99
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	107.080, 111.760, 161.440, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 22.2

The binding sites of Zinc atom in the E.Coli Qued, Semet Protein, 2A Resolution (pdb code 4ntn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the E.Coli Qued, Semet Protein, 2A Resolution, PDB code: 4ntn:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in the E.Coli Qued, Semet Protein, 2A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of E.Coli Qued, Semet Protein, 2A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:30.9 occ:1.00 O A:HOH302 2.0 22.0 1.0 NE2 A:HIS16 2.1 31.3 1.0 NE2 A:HIS31 2.1 30.6 1.0 NE2 A:HIS33 2.1 31.7 1.0 CE1 A:HIS16 3.0 31.2 1.0 CD2 A:HIS33 3.0 30.3 1.0 CD2 A:HIS31 3.0 30.9 1.0 CD2 A:HIS16 3.1 31.2 1.0 CE1 A:HIS31 3.1 30.6 1.0 CE1 A:HIS33 3.2 32.2 1.0 OE1 A:GLU110 4.0 53.0 1.0 ND1 A:HIS16 4.1 31.4 1.0 CG A:HIS31 4.2 30.7 1.0 CG A:HIS33 4.2 30.7 1.0 ND1 A:HIS31 4.2 31.0 1.0 CG A:HIS16 4.2 30.8 1.0 ND1 A:HIS33 4.2 32.4 1.0 CD A:GLU110 4.5 50.0 1.0 NE2 C:HIS71 4.6 35.0 1.0 CD2 C:HIS71 4.8 34.8 1.0 SG A:CYS27 4.8 43.2 1.0

Zinc binding site 2 out of 6 in the E.Coli Qued, Semet Protein, 2A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of E.Coli Qued, Semet Protein, 2A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:30.3 occ:1.00 O B:HOH303 2.0 19.4 1.0 NE2 B:HIS16 2.1 26.3 1.0 NE2 B:HIS31 2.1 28.1 1.0 NE2 B:HIS33 2.2 29.1 1.0 CD2 B:HIS33 2.9 28.2 1.0 CE1 B:HIS31 3.0 27.7 1.0 CE1 B:HIS16 3.0 25.8 1.0 CD2 B:HIS16 3.1 26.4 1.0 CD2 B:HIS31 3.1 28.4 1.0 CE1 B:HIS33 3.3 29.6 1.0 ND1 B:HIS31 4.1 28.1 1.0 ND1 B:HIS16 4.2 25.8 1.0 CG B:HIS33 4.2 28.2 1.0 CG B:HIS31 4.2 28.1 1.0 CG B:HIS16 4.2 26.5 1.0 CD B:GLU110 4.2 46.6 1.0 OE2 B:GLU110 4.3 50.4 1.0 ND1 B:HIS33 4.3 28.9 1.0 OE1 B:GLU110 4.3 49.5 1.0 NE2 D:HIS71 4.8 35.9 1.0 CG B:GLU110 4.8 43.0 1.0 SG B:CYS27 4.8 38.1 1.0 CD2 D:HIS71 4.9 35.6 1.0

Zinc binding site 3 out of 6 in the E.Coli Qued, Semet Protein, 2A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of E.Coli Qued, Semet Protein, 2A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn201 b:32.9 occ:1.00 NE2 C:HIS31 2.1 31.5 1.0 O C:HOH302 2.1 27.8 1.0 NE2 C:HIS16 2.1 29.0 1.0 NE2 C:HIS33 2.2 31.4 1.0 CD2 C:HIS33 3.0 29.9 1.0 CD2 C:HIS31 3.1 31.0 1.0 CE1 C:HIS31 3.1 30.9 1.0 CD2 C:HIS16 3.1 28.9 1.0 CE1 C:HIS16 3.1 29.4 1.0 CE1 C:HIS33 3.2 30.3 1.0 OE2 C:GLU110 3.6 54.0 1.0 CD C:GLU110 3.7 49.7 1.0 ND1 C:HIS31 4.2 31.2 1.0 CG C:GLU110 4.2 46.6 1.0 OE1 C:GLU110 4.2 50.3 1.0 CG C:HIS31 4.2 30.8 1.0 ND1 C:HIS16 4.2 30.1 1.0 CG C:HIS33 4.2 30.4 1.0 CG C:HIS16 4.2 29.7 1.0 ND1 C:HIS33 4.3 30.7 1.0 SG C:CYS27 4.7 47.9 1.0 NE2 A:HIS71 4.8 35.6 1.0 CD2 A:HIS71 4.9 35.8 1.0

Zinc binding site 4 out of 6 in the E.Coli Qued, Semet Protein, 2A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of E.Coli Qued, Semet Protein, 2A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:30.7 occ:1.00 NE2 D:HIS16 2.1 27.7 1.0 NE2 D:HIS31 2.1 27.7 1.0 O D:HOH302 2.2 22.6 1.0 NE2 D:HIS33 2.2 28.3 1.0 CD2 D:HIS33 3.0 27.8 1.0 CE1 D:HIS31 3.0 27.9 1.0 CE1 D:HIS16 3.1 27.8 1.0 CD2 D:HIS16 3.1 27.2 1.0 CD2 D:HIS31 3.1 27.8 1.0 CE1 D:HIS33 3.2 28.0 1.0 OE2 D:GLU110 4.1 50.7 1.0 ND1 D:HIS31 4.2 28.2 1.0 CG D:HIS33 4.2 27.4 1.0 ND1 D:HIS16 4.2 28.3 1.0 CG D:HIS31 4.2 28.0 1.0 CG D:HIS16 4.3 28.1 1.0 ND1 D:HIS33 4.3 28.4 1.0 OE1 D:GLU110 4.3 46.6 1.0 CD D:GLU110 4.4 47.1 1.0 NE2 B:HIS71 4.7 30.5 1.0 SG D:CYS27 4.8 41.6 1.0 CD2 B:HIS71 4.8 30.8 1.0

Zinc binding site 5 out of 6 in the E.Coli Qued, Semet Protein, 2A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of E.Coli Qued, Semet Protein, 2A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn201 b:31.4 occ:1.00 NE2 E:HIS16 2.1 28.5 1.0 O E:HOH302 2.1 25.9 1.0 NE2 E:HIS31 2.1 30.8 1.0 NE2 E:HIS33 2.1 30.3 1.0 CE1 E:HIS16 3.0 28.5 1.0 CD2 E:HIS31 3.0 30.4 1.0 CD2 E:HIS33 3.0 29.7 1.0 CD2 E:HIS16 3.1 28.4 1.0 CE1 E:HIS31 3.1 30.0 1.0 CE1 E:HIS33 3.2 30.6 1.0 OE1 E:GLU110 4.2 46.6 1.0 ND1 E:HIS16 4.2 28.2 1.0 ND1 E:HIS31 4.2 30.2 1.0 CG E:HIS31 4.2 30.3 1.0 CG E:HIS16 4.2 28.9 1.0 CG E:HIS33 4.2 29.8 1.0 ND1 E:HIS33 4.2 30.6 1.0 CD E:GLU110 4.3 43.7 1.0 OE2 E:GLU110 4.3 47.3 1.0 SG E:CYS27 4.8 40.9 1.0 NE2 F:HIS71 4.8 37.1 1.0 CD2 F:HIS71 5.0 36.7 1.0

Zinc binding site 6 out of 6 in the E.Coli Qued, Semet Protein, 2A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of E.Coli Qued, Semet Protein, 2A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn201 b:32.5 occ:1.00 NE2 F:HIS31 2.0 31.8 1.0 NE2 F:HIS16 2.1 31.2 1.0 O F:HOH302 2.2 23.8 1.0 NE2 F:HIS33 2.3 29.9 1.0 CE1 F:HIS31 2.9 32.2 1.0 CD2 F:HIS33 3.0 30.2 1.0 CD2 F:HIS31 3.0 31.6 1.0 CE1 F:HIS16 3.1 31.7 1.0 CD2 F:HIS16 3.1 31.2 1.0 CE1 F:HIS33 3.4 30.0 1.0 ND1 F:HIS31 4.1 32.2 1.0 CD F:GLU110 4.1 46.8 1.0 CG F:HIS31 4.1 32.2 1.0 OE1 F:GLU110 4.2 50.0 1.0 ND1 F:HIS16 4.2 31.9 1.0 CG F:HIS33 4.2 30.2 1.0 CG F:HIS16 4.3 31.9 1.0 OE2 F:GLU110 4.3 50.0 1.0 ND1 F:HIS33 4.4 30.5 1.0 CG F:GLU110 4.4 44.9 1.0 NE2 E:HIS71 4.6 36.2 1.0 SG F:CYS27 4.7 49.6 1.0 CD2 E:HIS71 4.8 36.6 1.0

Z.D.Miles, S.A.Roberts, R.M.Mccarty, V.Bandarian. Biochemical and Structural Studies of 6-Carboxy-5,6,7,8-Tetrahydropterin Synthase Reveal the Molecular Basis of Catalytic Promiscuity Within the Tunnel-Fold Superfamily. J.Biol.Chem. V. 289 23641 2014.
ISSN: ISSN 0021-9258
PubMed: 24990950
DOI: 10.1074/JBC.M114.555680