Zinc in PDB 1gs8: Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase

All present enzymatic activity of Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase:
1.7.2.1; 1.7.99.3;

The structure of Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs8 was solved by M.J.Ellis, M.Prudencio, F.E.Dodd, R.W.Strange, G.Sawers, R.R.Eady, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	68.97 / 1.9
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	79.636, 79.636, 99.867, 90.00, 90.00, 120.00
R / Rfree (%)	16.5 / 20.7

The structure of Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase also contains other interesting chemical elements:

Copper

(Cu)

2 atoms

The binding sites of Zinc atom in the Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase (pdb code 1gs8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase, PDB code: 1gs8:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase


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 Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1339 b:20.4 occ:0.75 OD2 A:ASP167 2.1 18.0 1.0 O A:HOH2251 2.2 21.7 1.0 NE2 A:HIS165 2.2 25.4 1.0 O A:HOH2252 2.4 26.3 1.0 CG A:ASP167 2.7 18.9 1.0 OD1 A:ASP167 2.8 18.4 1.0 CE1 A:HIS165 3.1 26.1 1.0 CD2 A:HIS165 3.3 22.9 1.0 OG1 A:THR234 3.9 18.7 1.0 N A:THR234 4.1 17.3 1.0 O A:GLY232 4.1 18.0 1.0 CB A:ASP167 4.2 17.1 1.0 ND1 A:HIS165 4.3 24.8 1.0 CB A:THR234 4.3 16.1 1.0 CG A:HIS165 4.4 23.4 1.0 CA A:GLU233 4.7 17.9 1.0 N A:ASP167 4.8 17.8 1.0 C A:GLU233 4.8 17.4 1.0 CA A:THR234 4.8 17.2 1.0 CA A:ASP167 5.0 17.4 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase


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 Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1340 b:21.7 occ:0.75 O A:HOH2254 1.9 15.0 1.0 OD2 A:ASP73 2.1 15.0 1.0 ND1 A:HIS70 2.4 17.5 1.0 O A:HOH2253 2.4 14.3 1.0 CG A:ASP73 3.1 14.6 1.0 CG A:HIS70 3.3 17.3 1.0 CE1 A:HIS70 3.4 18.7 1.0 OD1 A:ASP73 3.4 16.6 1.0 CB A:HIS70 3.5 14.4 1.0 N A:HIS70 3.5 15.2 1.0 CA A:HIS70 4.1 14.9 1.0 O A:HOH2071 4.3 31.9 1.0 C A:VAL69 4.3 15.6 1.0 CB A:ASP73 4.4 13.8 1.0 NE2 A:HIS70 4.5 17.8 1.0 CD2 A:HIS70 4.5 16.2 1.0 NH1 A:ARG153 4.5 18.4 1.0 CA A:VAL69 4.5 14.5 1.0 CG2 A:VAL33 4.6 14.5 1.0 NH2 A:ARG153 4.7 19.1 1.0 CB A:VAL69 4.9 13.4 1.0 O A:HOH2030 4.9 18.6 1.0 O A:HIS70 5.0 14.7 1.0 C A:HIS70 5.0 15.7 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Mutant D92N Alcaligenes Xylosoxidans Nitrite Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1341 b:27.4 occ:0.50 NE2 A:HIS8 2.0 28.8 1.0 CE1 A:HIS8 2.7 28.5 1.0 CD2 A:HIS8 3.0 26.6 1.0 O A:ASP4 3.7 29.9 1.0 ND1 A:HIS8 3.8 27.8 1.0 CG A:HIS8 3.9 25.3 1.0 C A:ASP4 4.2 29.4 1.0 O A:LEU6 4.2 17.5 1.0 O A:ALA3 4.3 26.3 1.0 O A:HOH2077 4.3 23.6 1.0 CA A:ASP4 4.4 29.9 1.0 O A:HOH2078 4.5 32.6 1.0

M.J.Ellis, M.Prudencio, F.E.Dodd, R.W.Strange, G.Sawers, R.R.Eady, S.S.Hasnain. Biochemical and Crystallographic Studies of the MET144ALA, ASP92ASN and HIS254PHE Mutants of the Nitrite Reductase From Alcaligenes Xylosoxidans Provide Insight Into the Enzyme Mechanism. J.Mol.Biol. V. 316 51 2002.
ISSN: ISSN 0022-2836
PubMed: 11829502
DOI: 10.1006/JMBI.2001.5304