Zinc in PDB 5hmf: Crystal Structure of Triazine Hydrolase Variant (P214T/Y215H/E241Q)

All present enzymatic activity of Crystal Structure of Triazine Hydrolase Variant (P214T/Y215H/E241Q):
3.8.1.8;

The structure of Crystal Structure of Triazine Hydrolase Variant (P214T/Y215H/E241Q), PDB code: 5hmf 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)	45.97 / 1.84
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.250, 101.670, 80.430, 90.00, 104.02, 90.00
R / Rfree (%)	16.4 / 19.5

The binding sites of Zinc atom in the Crystal Structure of Triazine Hydrolase Variant (P214T/Y215H/E241Q) (pdb code 5hmf). 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 (P214T/Y215H/E241Q), PDB code: 5hmf:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Triazine Hydrolase Variant (P214T/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 (P214T/Y215H/E241Q) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:17.6 occ:0.79 NE2 A:HIS63 2.2 15.0 1.0 NE2 A:HIS238 2.2 20.2 1.0 O A:HOH797 2.2 16.2 1.0 NE2 A:HIS65 2.3 18.6 1.0 CE1 A:HIS65 3.1 23.2 1.0 CD2 A:HIS63 3.2 10.3 1.0 CD2 A:HIS238 3.2 10.0 1.0 HE1 A:HIS65 3.2 27.9 1.0 CE1 A:HIS63 3.2 22.8 1.0 CE1 A:HIS238 3.2 15.5 1.0 HD2 A:HIS63 3.3 12.4 1.0 HD2 A:HIS238 3.3 12.0 1.0 CD2 A:HIS65 3.3 18.2 1.0 HE1 A:HIS63 3.4 27.4 1.0 HE1 A:HIS238 3.4 18.6 1.0 HD2 A:HIS65 3.6 21.8 1.0 HG22 A:THR325 3.7 21.2 1.0 HB A:THR325 3.7 13.5 1.0 OE1 A:GLN129 4.1 15.1 1.0 O A:HOH803 4.1 27.9 1.0 HG21 A:THR325 4.2 21.2 1.0 ND1 A:HIS65 4.2 20.3 1.0 CG2 A:THR325 4.3 17.6 1.0 ND1 A:HIS63 4.3 15.0 1.0 CG A:HIS63 4.3 12.7 1.0 NE2 A:HIS274 4.3 12.3 1.0 ND1 A:HIS238 4.3 14.9 1.0 CG A:HIS238 4.3 14.0 1.0 O A:HOH763 4.4 22.2 1.0 CG A:HIS65 4.4 12.4 1.0 CB A:THR325 4.4 11.3 1.0 O A:HOH915 4.5 26.3 1.0 HA A:THR325 4.7 10.0 1.0 H A:GLY326 4.8 12.6 1.0 O A:HOH722 4.8 13.2 1.0 HB1 A:ALA273 4.9 14.4 1.0 HD2 A:HIS274 4.9 22.9 1.0 HD1 A:HIS65 5.0 24.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Triazine Hydrolase Variant (P214T/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 (P214T/Y215H/E241Q) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:22.4 occ:0.91 NE2 B:HIS63 2.2 17.4 1.0 NE2 B:HIS65 2.2 17.1 1.0 NE2 B:HIS238 2.3 21.3 1.0 O B:HOH768 2.3 19.2 1.0 HE1 B:HIS65 2.7 30.0 1.0 CE1 B:HIS65 2.8 25.0 1.0 CE1 B:HIS63 3.1 22.1 1.0 CD2 B:HIS63 3.2 20.6 1.0 CD2 B:HIS238 3.2 18.6 1.0 CE1 B:HIS238 3.2 19.2 1.0 HE1 B:HIS63 3.3 26.5 1.0 HD2 B:HIS238 3.4 22.3 1.0 HE1 B:HIS238 3.4 23.0 1.0 HD2 B:HIS63 3.4 24.7 1.0 CD2 B:HIS65 3.4 22.8 1.0 HB B:THR325 3.8 12.9 1.0 HD2 B:HIS65 3.8 27.3 1.0 OE1 B:GLN129 3.9 26.9 1.0 ND1 B:HIS65 4.0 21.7 1.0 HG22 B:THR325 4.1 17.0 1.0 ND1 B:HIS63 4.3 25.1 1.0 HG21 B:THR325 4.3 17.0 1.0 CG B:HIS63 4.3 14.1 1.0 ND1 B:HIS238 4.4 22.0 1.0 CG B:HIS65 4.4 20.1 1.0 NE2 B:HIS274 4.4 14.2 1.0 CG B:HIS238 4.4 13.9 1.0 HG2 B:GLN129 4.4 43.8 1.0 CG2 B:THR325 4.5 14.2 1.0 CB B:THR325 4.6 10.8 1.0 HA B:THR325 4.7 14.6 1.0 HD1 B:HIS65 4.7 26.1 1.0 CD B:GLN129 4.8 35.8 1.0 O B:HOH728 4.9 11.3 1.0 HB1 B:ALA273 4.9 17.2 1.0 HD13 B:LEU296 4.9 23.9 1.0 HD2 B:HIS274 4.9 18.6 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