Zinc in PDB 1et8: Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis

All present enzymatic activity of Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis:
1.7.99.3;

The structure of Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis, PDB code: 1et8 was solved by M.J.Boulanger, M.Kukimoto, M.Nishiyama, S.Horinouchi, M.E.P.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	500.00 / 1.80
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	127.659, 127.659, 67.215, 90.00, 90.00, 120.00
R / Rfree (%)	18.2 / 21.2

The structure of Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis also contains other interesting chemical elements:

Copper

(Cu)

2 atoms

The binding sites of Zinc atom in the Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis (pdb code 1et8). 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 Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis, PDB code: 1et8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis


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 Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn504 b:40.5 occ:0.33 O A:HOH661 2.1 40.6 1.0 O A:HOH625 2.2 33.8 1.0 O A:HOH788 4.2 45.6 1.0 OD1 A:ASP275 4.2 27.3 1.0 O A:HOH801 4.4 48.8 1.0 OD2 A:ASP275 4.6 27.5 1.0 CG A:ASP275 4.9 26.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis


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 Nitrite Reductase HIS255ASN Mutant From Alcaligenes Faecalis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn505 b:45.9 occ:1.00 O A:HOH732 2.0 46.5 1.0 OE2 A:GLU89 2.1 41.4 1.0 CD A:GLU89 2.9 40.8 1.0 OE1 A:GLU89 2.9 42.4 1.0 CG A:GLU89 4.3 38.1 1.0

M.J.Boulanger, M.Kukimoto, M.Nishiyama, S.Horinouchi, M.E.Murphy. Catalytic Roles For Two Water Bridged Residues (Asp-98 and His-255) in the Active Site of Copper-Containing Nitrite Reductase. J.Biol.Chem. V. 275 23957 2000.
ISSN: ISSN 0021-9258
PubMed: 10811642
DOI: 10.1074/JBC.M001859200