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

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

The structure of Crystal Structure of Triazine Hydrolase Variant (P214T/Y215H), PDB code: 5hme 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)	35.98 / 2.15
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.551, 100.718, 78.851, 90.00, 102.30, 90.00
R / Rfree (%)	20.3 / 22.7

The binding sites of Zinc atom in the Crystal Structure of Triazine Hydrolase Variant (P214T/Y215H) (pdb code 5hme). 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), PDB code: 5hme:
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)


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) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:30.0 occ:1.00 HE1 A:HIS238 1.7 39.6 1.0 HE2 A:HIS63 1.7 16.5 1.0 NE2 A:HIS63 2.3 16.5 1.0 NE2 A:HIS65 2.4 16.8 1.0 CE1 A:HIS238 2.4 33.0 1.0 O A:HOH759 2.5 27.2 1.0 CE1 A:HIS63 3.1 11.0 1.0 HG1 A:THR325 3.1 25.3 1.0 HE1 A:HIS63 3.1 13.2 1.0 NE2 A:HIS238 3.3 21.9 1.0 CE1 A:HIS65 3.3 13.9 1.0 CD2 A:HIS63 3.3 19.7 1.0 OG1 A:THR325 3.4 21.1 1.0 ND1 A:HIS238 3.4 23.9 1.0 CD2 A:HIS65 3.4 13.1 1.0 HE2 A:HIS238 3.4 21.9 1.0 HE1 A:HIS65 3.4 16.7 1.0 HD2 A:HIS65 3.5 15.7 1.0 HD2 A:HIS63 3.6 23.6 1.0 OE1 A:GLN129 3.9 16.6 1.0 O A:HOH750 4.0 27.2 1.0 ND1 A:HIS63 4.2 18.8 1.0 NE2 A:HIS274 4.3 18.1 1.0 CG A:HIS63 4.4 18.4 1.0 CD2 A:HIS238 4.4 17.4 1.0 ND1 A:HIS65 4.4 22.4 1.0 CG A:HIS238 4.4 23.2 1.0 CG A:HIS65 4.5 21.2 1.0 HA A:THR325 4.7 22.8 1.0 H A:GLY326 4.7 24.8 1.0 O A:HOH777 4.7 27.2 1.0 CB A:THR325 4.8 21.9 1.0 HB1 A:ALA273 4.8 19.9 1.0 HD2 A:HIS274 4.9 12.6 1.0 HD13 A:LEU296 5.0 19.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Triazine Hydrolase Variant (P214T/Y215H)


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) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:30.0 occ:0.67 HE1 B:HIS63 1.6 23.1 1.0 HE1 B:HIS238 2.1 21.1 1.0 CE1 B:HIS63 2.3 19.3 1.0 NE2 B:HIS65 2.5 28.3 1.0 O B:HOH751 2.7 30.0 1.0 CE1 B:HIS238 2.7 17.6 1.0 HE1 B:HIS65 3.0 26.8 1.0 CE1 B:HIS65 3.1 22.3 1.0 NE2 B:HIS63 3.1 13.9 1.0 HE2 B:HIS238 3.2 32.9 1.0 NE2 B:HIS238 3.3 32.9 1.0 ND1 B:HIS63 3.3 34.4 1.0 HD1 B:HIS63 3.5 34.4 1.0 OE1 B:GLN129 3.6 42.6 1.0 CD2 B:HIS65 3.6 19.3 1.0 ND1 B:HIS238 3.8 19.5 1.0 HB B:THR325 3.8 33.8 1.0 HG22 B:THR325 3.8 35.3 1.0 HD2 B:HIS65 3.9 23.1 1.0 O B:HOH771 4.0 27.2 1.0 HG2 B:GLN129 4.0 49.1 1.0 HD1 B:HIS238 4.1 19.5 1.0 HG21 B:THR325 4.2 35.3 1.0 CD2 B:HIS63 4.2 20.0 1.0 CD B:GLN129 4.3 40.0 1.0 ND1 B:HIS65 4.3 28.3 1.0 CG B:HIS63 4.3 14.4 1.0 CG2 B:THR325 4.3 29.4 1.0 NE2 B:HIS274 4.4 20.6 1.0 CD2 B:HIS238 4.4 15.6 1.0 CB B:THR325 4.5 28.1 1.0 CG B:GLN129 4.6 41.0 1.0 CG B:HIS65 4.6 18.3 1.0 HG3 B:GLN129 4.7 49.1 1.0 CG B:HIS238 4.7 23.0 1.0 HA B:THR325 4.7 26.3 1.0 HD2 B:HIS274 4.9 32.7 1.0 HD13 B:LEU296 5.0 28.0 1.0 HD1 B:HIS65 5.0 28.3 1.0 HB1 B:ALA273 5.0 22.0 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