Zinc in PDB 5hmd: Crystal Structure of Triazine Hydrolase Variant (Y215H/E241Q)

All present enzymatic activity of Crystal Structure of Triazine Hydrolase Variant (Y215H/E241Q):
3.8.1.8;

The structure of Crystal Structure of Triazine Hydrolase Variant (Y215H/E241Q), PDB code: 5hmd was solved by E.Sugrue, P.D.Carr, C.J.Jackson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.69 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.154, 99.415, 77.183, 90.00, 101.12, 90.00
R / Rfree (%)	14.5 / 20.3

The binding sites of Zinc atom in the Crystal Structure of Triazine Hydrolase Variant (Y215H/E241Q) (pdb code 5hmd). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Triazine Hydrolase Variant (Y215H/E241Q), PDB code: 5hmd:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Triazine Hydrolase Variant (Y215H/E241Q)


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 Triazine Hydrolase Variant (Y215H/E241Q) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:20.9 occ:1.00 NE2 A:HIS65 2.2 18.1 1.0 NE2 A:HIS63 2.2 13.7 1.0 NE2 A:HIS238 2.2 22.4 1.0 O A:HOH753 2.4 29.6 1.0 CE1 A:HIS65 3.0 18.4 1.0 HG1 A:THR325 3.1 46.4 1.0 CE1 A:HIS63 3.1 12.7 1.0 HE1 A:HIS65 3.1 22.1 1.0 CE1 A:HIS238 3.2 12.2 1.0 CD2 A:HIS238 3.2 19.2 1.0 HE1 A:HIS63 3.2 15.2 1.0 CD2 A:HIS63 3.3 16.8 1.0 CD2 A:HIS65 3.3 15.4 1.0 HE1 A:HIS238 3.3 14.6 1.0 OG1 A:THR325 3.3 38.7 1.0 HD2 A:HIS238 3.4 23.0 1.0 HD2 A:HIS63 3.5 20.2 1.0 HD2 A:HIS65 3.5 18.5 1.0 O A:HOH819 3.7 36.2 1.0 ND1 A:HIS65 4.2 20.9 1.0 ND1 A:HIS63 4.3 22.6 1.0 ND1 A:HIS238 4.3 14.8 1.0 OE1 A:GLN129 4.3 13.9 1.0 NE2 A:HIS274 4.3 17.0 1.0 CG A:HIS65 4.3 16.7 1.0 CG A:HIS238 4.3 16.2 1.0 CG A:HIS63 4.4 22.5 1.0 O A:HOH739 4.6 20.4 1.0 H A:GLY326 4.6 16.0 1.0 CB A:THR325 4.8 21.4 1.0 HA A:THR325 4.8 18.7 1.0 HB1 A:ALA273 4.9 15.2 1.0 HD13 A:LEU296 4.9 20.3 1.0 HD1 A:HIS65 5.0 25.1 1.0 O A:HOH800 5.0 19.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Triazine Hydrolase Variant (Y215H/E241Q)


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 Triazine Hydrolase Variant (Y215H/E241Q) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:26.3 occ:1.00 NE2 B:HIS63 2.2 16.4 1.0 NE2 B:HIS65 2.2 16.6 1.0 NE2 B:HIS238 2.3 19.5 1.0 O B:HOH708 2.3 23.4 1.0 CE1 B:HIS65 2.9 27.3 1.0 HE1 B:HIS65 3.0 32.8 1.0 CE1 B:HIS63 3.1 22.2 1.0 HE1 B:HIS63 3.2 26.6 1.0 CD2 B:HIS238 3.2 24.0 1.0 CE1 B:HIS238 3.2 24.6 1.0 CD2 B:HIS63 3.2 13.5 1.0 CD2 B:HIS65 3.3 15.7 1.0 HD2 B:HIS238 3.4 28.8 1.0 HE1 B:HIS238 3.4 29.5 1.0 HD2 B:HIS63 3.5 16.2 1.0 HD2 B:HIS65 3.6 18.8 1.0 HB B:THR325 3.7 18.5 1.0 OE1 B:GLN129 4.1 33.0 1.0 ND1 B:HIS65 4.1 21.9 1.0 HG22 B:THR325 4.2 22.8 1.0 ND1 B:HIS63 4.2 31.9 1.0 CG B:HIS65 4.3 12.2 1.0 CG B:HIS63 4.3 14.3 1.0 ND1 B:HIS238 4.4 23.4 1.0 CG B:HIS238 4.4 21.7 1.0 NE2 B:HIS274 4.4 20.2 1.0 HG21 B:THR325 4.5 22.8 1.0 CB B:THR325 4.6 15.4 1.0 CG2 B:THR325 4.6 19.0 1.0 O B:HOH729 4.7 16.3 1.0 HA B:THR325 4.8 17.4 1.0 HD1 B:HIS65 4.8 26.3 1.0 HB1 B:ALA273 4.9 16.6 1.0 H B:GLY326 4.9 15.8 1.0 HD2 B:HIS274 5.0 25.0 1.0 HD13 B:LEU296 5.0 18.2 1.0 HD1 B:HIS63 5.0 38.3 1.0 HB3 B:GLN129 5.0 28.1 1.0

E.Sugrue, P.D.Carr, C.Scott, C.J.Jackson. Active Site Desolvation and Thermostability Trade-Offs in the Evolution of Catalytically Diverse Triazine Hydrolases. Biochemistry V. 55 6304 2016.
ISSN: ISSN 1520-4995
PubMed: 27768291
DOI: 10.1021/ACS.BIOCHEM.6B00731