Zinc in PDB 4p9e: Crystal Structure of Dcmp Deaminase From the Cyanophage S-TIM5 in Apo Form

The structure of Crystal Structure of Dcmp Deaminase From the Cyanophage S-TIM5 in Apo Form, PDB code: 4p9e was solved by A.Marx, A.Alian, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	67.66 / 2.60
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	78.130, 78.130, 80.560, 90.00, 90.00, 120.00
R / Rfree (%)	21.2 / 27.2

The structure of Crystal Structure of Dcmp Deaminase From the Cyanophage S-TIM5 in Apo Form also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Dcmp Deaminase From the Cyanophage S-TIM5 in Apo Form (pdb code 4p9e). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Dcmp Deaminase From the Cyanophage S-TIM5 in Apo Form, PDB code: 4p9e:

Zinc binding site 1 out of 1 in the Crystal Structure of Dcmp Deaminase From the Cyanophage S-TIM5 in Apo Form


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 Dcmp Deaminase From the Cyanophage S-TIM5 in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:54.5 occ:1.00 ND1 A:HIS67 2.0 47.7 1.0 SG A:CYS95 2.2 48.7 1.0 SG A:CYS98 2.3 50.4 1.0 O A:HOH311 2.4 62.0 1.0 CE1 A:HIS67 2.8 41.3 1.0 CG A:HIS67 3.1 46.0 1.0 CB A:CYS95 3.1 54.3 1.0 CB A:CYS98 3.2 48.6 1.0 CB A:HIS67 3.6 38.0 1.0 N A:CYS95 3.6 48.0 1.0 CA A:CYS95 3.9 53.8 1.0 NE2 A:HIS67 3.9 42.1 1.0 N A:CYS98 4.0 47.6 1.0 O A:HOH312 4.0 64.1 1.0 CD2 A:HIS67 4.1 47.4 1.0 CA A:CYS98 4.2 43.6 1.0 OE1 A:GLU69 4.3 42.6 1.0 OE2 A:GLU69 4.4 47.9 1.0 CD A:GLU69 4.5 46.4 1.0 C A:CYS95 4.5 51.7 1.0 O A:CYS95 4.6 50.3 1.0 C A:PRO94 4.7 47.5 1.0 NE2 A:GLN70 4.8 51.0 1.0 CA A:PRO94 5.0 50.1 1.0

A.Marx, A.Alian. The First Crystal Structure of A Dttp Bound Deoxycytidylate Deaminase Validates and Details the Allosteric-Inhibitor Binding Site J.Biol.Chem. 2014.
ISSN: ESSN 1083-351X
DOI: 10.1074/JBC.M114.617720