Zinc in PDB 5ltz: GMHA_MUTANT Q175E

All present enzymatic activity of GMHA_MUTANT Q175E:
5.3.1.28;

The structure of GMHA_MUTANT Q175E, PDB code: 5ltz was solved by M.Vivoli, N.J.Harmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.25 / 1.67
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	72.550, 84.473, 126.682, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 24.5

The structure of GMHA_MUTANT Q175E also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Zinc atom in the GMHA_MUTANT Q175E (pdb code 5ltz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the GMHA_MUTANT Q175E, PDB code: 5ltz:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the GMHA_MUTANT Q175E


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of GMHA_MUTANT Q175E within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn202 b:25.1 occ:0.71 OE2 A:GLU68 1.8 28.2 0.5 OE1 D:GLU175 2.1 26.6 1.0 OE2 A:GLU68 2.1 29.9 0.5 NE2 A:HIS183 2.2 25.4 1.0 NE2 A:HIS64 2.2 27.1 1.0 O2 A:I22205 2.5 32.9 0.8 O1 A:I22205 2.6 34.1 0.8 CD D:GLU175 3.0 28.4 1.0 CD2 A:HIS64 3.1 26.2 1.0 CD A:GLU68 3.1 27.8 0.5 CD2 A:HIS183 3.1 23.5 1.0 CE1 A:HIS183 3.2 22.6 1.0 CE1 A:HIS64 3.3 24.3 1.0 CD A:GLU68 3.3 29.7 0.5 C2 A:I22205 3.3 32.5 0.8 OE2 D:GLU175 3.4 28.7 1.0 C1 A:I22205 3.5 31.7 0.8 OE1 A:GLU68 3.9 31.5 0.5 OE1 A:GLU68 3.9 33.0 0.5 CG A:GLU68 4.0 28.3 0.5 ND1 A:HIS183 4.3 24.3 1.0 CG A:HIS183 4.3 26.3 1.0 CG A:HIS64 4.3 24.5 1.0 ND1 A:HIS64 4.3 23.2 1.0 CG D:GLU175 4.4 25.1 1.0 CG A:GLU68 4.5 32.0 0.5 CA D:GLY57 4.6 24.5 1.0 CB D:GLU175 4.6 24.2 1.0 C3 A:I22205 4.8 33.1 0.8 CA D:PRO172 4.9 27.6 1.0 CD1 A:LEU179 4.9 25.8 1.0

Zinc binding site 2 out of 4 in the GMHA_MUTANT Q175E


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of GMHA_MUTANT Q175E within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn204 b:25.7 occ:0.74 OE1 D:GLU68 1.8 34.5 1.0 OE1 A:GLU175 2.0 25.2 1.0 NE2 D:HIS64 2.1 24.8 1.0 NE2 D:HIS183 2.1 24.1 1.0 O2 A:I22203 2.5 35.7 1.0 CD A:GLU175 3.0 27.4 1.0 CD D:GLU68 3.0 33.5 1.0 C1 A:I22203 3.1 39.5 1.0 CE1 D:HIS183 3.1 23.3 1.0 CD2 D:HIS64 3.1 27.0 1.0 CD2 D:HIS183 3.1 25.1 1.0 CE1 D:HIS64 3.1 27.2 1.0 C2 A:I22203 3.2 38.5 1.0 OE2 A:GLU175 3.4 27.6 1.0 OE2 D:GLU68 3.7 43.8 1.0 CG D:GLU68 4.2 36.8 1.0 ND1 D:HIS183 4.2 22.3 1.0 ND1 D:HIS64 4.2 24.6 1.0 CG D:HIS183 4.2 22.8 1.0 CG D:HIS64 4.2 23.5 1.0 O1 A:I22203 4.3 47.0 1.0 CG A:GLU175 4.3 24.2 1.0 CB A:GLU175 4.6 25.3 1.0 CA A:GLY57 4.6 22.1 1.0 CE1 D:PHE73 4.6 33.3 1.0 CA A:PRO172 4.6 25.9 1.0 C3 A:I22203 4.7 40.7 1.0 CB A:PRO172 4.9 30.9 1.0 CD1 D:LEU179 4.9 28.0 1.0

Zinc binding site 3 out of 4 in the GMHA_MUTANT Q175E


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of GMHA_MUTANT Q175E within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn203 b:33.3 occ:0.70 OE1 C:GLU175 2.0 30.7 1.0 NE2 B:HIS64 2.1 33.7 1.0 OE1 B:GLU68 2.1 36.1 1.0 NE2 B:HIS183 2.2 32.6 1.0 O1 B:I22206 2.5 43.3 1.0 O2 B:I22206 2.6 40.3 1.0 CD C:GLU175 2.9 33.4 1.0 CE1 B:HIS64 3.1 31.8 1.0 CD2 B:HIS64 3.1 32.3 1.0 CD2 B:HIS183 3.2 31.8 1.0 CD B:GLU68 3.2 43.1 1.0 CE1 B:HIS183 3.2 34.0 1.0 OE2 C:GLU175 3.3 33.0 1.0 C2 B:I22206 3.4 40.9 1.0 C1 B:I22206 3.5 40.1 1.0 OE2 B:GLU68 3.7 46.9 1.0 ND1 B:HIS64 4.2 29.6 1.0 CG B:HIS64 4.2 28.2 1.0 ND1 B:HIS183 4.3 28.2 1.0 CG B:HIS183 4.3 31.8 1.0 CG C:GLU175 4.3 31.8 1.0 CG B:GLU68 4.4 41.7 1.0 CB C:GLU175 4.5 28.7 1.0 CA C:GLY57 4.5 29.3 1.0 CE1 B:PHE73 4.7 44.0 1.0 CA C:PRO172 4.7 31.7 1.0 C3 B:I22206 4.9 40.3 1.0 CB C:PRO172 5.0 36.5 1.0 CD1 B:PHE73 5.0 47.4 1.0

Zinc binding site 4 out of 4 in the GMHA_MUTANT Q175E


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of GMHA_MUTANT Q175E within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn205 b:29.3 occ:0.77 OE2 C:GLU68 1.8 38.1 1.0 OE1 B:GLU175 2.0 27.6 1.0 NE2 C:HIS183 2.2 29.7 1.0 NE2 C:HIS64 2.2 28.2 1.0 O1 B:I22204 2.3 39.8 1.0 O2 B:I22204 2.6 34.5 1.0 CD B:GLU175 2.9 29.8 1.0 CD C:GLU68 3.0 33.6 1.0 CE1 C:HIS183 3.1 22.7 1.0 CE1 C:HIS64 3.1 27.4 1.0 CD2 C:HIS64 3.1 28.5 1.0 CD2 C:HIS183 3.1 27.8 1.0 OE2 B:GLU175 3.2 28.5 1.0 C2 B:I22204 3.4 38.1 1.0 C1 B:I22204 3.4 34.7 1.0 OE1 C:GLU68 3.7 41.7 1.0 CG C:GLU68 4.1 35.4 1.0 ND1 C:HIS183 4.2 24.8 1.0 ND1 C:HIS64 4.2 30.6 1.0 CG C:HIS183 4.3 25.1 1.0 CG C:HIS64 4.3 25.9 1.0 CG B:GLU175 4.3 25.8 1.0 CA B:GLY57 4.5 25.2 1.0 CB B:GLU175 4.6 25.0 1.0 CE1 C:PHE73 4.6 34.9 1.0 CA B:PRO172 4.7 29.4 1.0 C3 B:I22204 4.8 36.4 1.0 CB B:PRO172 4.9 28.1 1.0

M.Vivoli, J.Pang, N.J.Harmer. A Half-Site Multimeric Enzyme Achieves Its Cooperativity Without Conformational Changes. Sci Rep V. 7 16529 2017.
ISSN: ESSN 2045-2322
PubMed: 29184087
DOI: 10.1038/S41598-017-16421-2