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Chlorine in PDB 9kws: D98N Mutant of A Copper-Containing Nitrite Reductase From Geobacillus Thermodenitrificans

Enzymatic activity of D98N Mutant of A Copper-Containing Nitrite Reductase From Geobacillus Thermodenitrificans

All present enzymatic activity of D98N Mutant of A Copper-Containing Nitrite Reductase From Geobacillus Thermodenitrificans:
1.7.2.1;

Protein crystallography data

The structure of D98N Mutant of A Copper-Containing Nitrite Reductase From Geobacillus Thermodenitrificans, PDB code: 9kws was solved by Y.Fukuda, M.Lintuluoto, Y.Hirano, K.Kusaka, T.Inoue, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.26 / 1.05
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 115.038, 115.038, 84.403, 90, 90, 120
R / Rfree (%) 9 / 10.1

Other elements in 9kws:

The structure of D98N Mutant of A Copper-Containing Nitrite Reductase From Geobacillus Thermodenitrificans also contains other interesting chemical elements:

Copper (Cu) 5 atoms
Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the D98N Mutant of A Copper-Containing Nitrite Reductase From Geobacillus Thermodenitrificans (pdb code 9kws). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the D98N Mutant of A Copper-Containing Nitrite Reductase From Geobacillus Thermodenitrificans, PDB code: 9kws:

Chlorine binding site 1 out of 1 in 9kws

Go back to Chlorine Binding Sites List in 9kws
Chlorine binding site 1 out of 1 in the D98N Mutant of A Copper-Containing Nitrite Reductase From Geobacillus Thermodenitrificans


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of D98N Mutant of A Copper-Containing Nitrite Reductase From Geobacillus Thermodenitrificans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl408

b:13.3
occ:0.72
CU A:CU402 2.3 9.2 1.0
HD22 A:ASN98 2.9 14.2 1.0
HE1 A:HIS134 3.2 10.4 0.9
NE2 A:HIS134 3.4 9.1 1.0
O A:HOH771 3.4 23.2 0.8
ND2 A:ASN98 3.4 11.8 1.0
O A:HOH899 3.4 23.5 0.4
HD21 A:ASN98 3.4 14.2 0.9
CE1 A:HIS134 3.6 8.7 1.0
NE2 A:HIS100 3.9 8.9 1.0
CG A:ASN98 4.5 10.4 1.0
O A:HOH657 4.6 12.4 1.0
CD2 A:HIS134 4.7 8.6 1.0
CD2 A:HIS100 4.7 8.5 1.0
HD2 A:HIS100 4.7 10.2 1.0
HG12 A:VAL140 4.8 12.6 0.7
CE1 A:HIS100 4.8 8.3 1.0
HE1 A:HIS100 4.8 10.0 1.0
O A:HOH894 4.8 30.0 0.9
O A:HOH771 4.8 16.0 0.2
H1 A:HOH657 4.9 14.9 1.0
OD1 A:ASN98 4.9 11.1 1.0
ND1 A:HIS134 4.9 8.8 1.0

Reference:

Y.Fukuda, M.Lintuluoto, Y.Hirano, K.Kusaka, T.Inoue, T.Tamada. Structural Basis of Cuproenzyme Nitrite Reduction at the Level of A Single Hydrogen Atom. J.Biol.Chem. 10290 2025.
ISSN: ESSN 1083-351X
PubMed: 40436316
DOI: 10.1016/J.JBC.2025.110290
Page generated: Sun Jul 13 17:11:29 2025

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