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Chlorine in PDB 3vkp: Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with Low X-Ray Dose

Enzymatic activity of Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with Low X-Ray Dose

All present enzymatic activity of Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with Low X-Ray Dose:
1.7.7.1;

Protein crystallography data

The structure of Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with Low X-Ray Dose, PDB code: 3vkp was solved by S.Nakano, M.Takahashi, A.Sakamoto, H.Morikawa, K.Katayanagi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.25 / 1.40
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 133.107, 133.107, 77.796, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 18.9

Other elements in 3vkp:

The structure of Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with Low X-Ray Dose also contains other interesting chemical elements:

Potassium (K) 1 atom
Iron (Fe) 5 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with Low X-Ray Dose (pdb code 3vkp). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with Low X-Ray Dose, PDB code: 3vkp:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 3vkp

Go back to Chlorine Binding Sites List in 3vkp
Chlorine binding site 1 out of 2 in the Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with Low X-Ray Dose


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with Low X-Ray Dose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl604

b:17.9
occ:1.00
O A:HOH1285 2.9 16.8 1.0
N A:MET175 3.0 10.4 1.0
O A:HOH1065 3.2 13.2 1.0
NH1 A:ARG179 3.6 9.8 1.0
CA A:MET175 3.7 10.6 1.0
CE2 A:PHE96 3.8 9.2 1.0
CMA A:SRM601 4.0 10.3 1.0
C A:GLY174 4.0 10.3 1.0
CG A:MET175 4.0 11.6 1.0
CA A:GLY174 4.0 10.0 1.0
O A:HOH1054 4.1 19.6 1.0
SD A:MET175 4.1 14.6 1.0
CD A:LYS91 4.2 12.8 1.0
CB A:MET175 4.4 11.3 1.0
CZ A:ARG179 4.5 8.3 1.0
CD2 A:PHE96 4.5 9.4 1.0
O A:HOH1908 4.6 15.7 1.0
O3D A:SRM601 4.7 13.2 1.0
CZ A:PHE96 4.7 9.2 1.0
NH2 A:ARG179 4.8 9.1 1.0
CE A:LYS91 4.9 14.3 1.0
C A:MET175 4.9 10.6 1.0
NZ A:LYS91 4.9 15.0 1.0
CHA A:SRM601 4.9 9.6 1.0
CG A:LYS91 4.9 11.4 1.0
O1 A:NO2606 4.9 16.6 1.0
O A:HOH1221 5.0 21.6 1.0
CB A:LYS91 5.0 10.7 1.0

Chlorine binding site 2 out of 2 in 3vkp

Go back to Chlorine Binding Sites List in 3vkp
Chlorine binding site 2 out of 2 in the Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with Low X-Ray Dose


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with Low X-Ray Dose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl605

b:18.5
occ:1.00
O A:HOH1133 3.1 15.3 1.0
O A:HOH1018 3.2 12.2 1.0
N A:LYS100 3.3 13.2 1.0
N A:ARG99 3.5 11.8 1.0
CB A:LYS100 3.8 14.7 1.0
CA A:GLY447 3.8 11.1 1.0
CB A:ARG99 4.1 12.6 1.0
CA A:ARG99 4.1 12.4 1.0
CA A:LYS100 4.1 14.2 1.0
C A:ARG98 4.2 11.4 1.0
C A:ARG99 4.2 13.1 1.0
N A:GLY447 4.2 10.6 1.0
O A:HIS97 4.3 11.5 1.0
O A:HOH1429 4.5 33.3 1.0
OE1 A:GLN448 4.5 19.3 0.5
CA A:ARG98 4.5 10.9 1.0
N A:ASN101 4.9 13.7 1.0
O A:ARG98 4.9 11.7 1.0
C A:GLY447 4.9 11.2 1.0
O A:HOH1528 5.0 30.7 1.0

Reference:

S.Nakano, M.Takahashi, A.Sakamoto, H.Morikawa, K.Katayanagi. The Reductive Reaction Mechanism of Tobacco Nitrite Reductase Derived From A Combination of Crystal Structures and Ultraviolet-Visible Microspectroscopy Proteins V. 80 2035 2012.
ISSN: ISSN 0887-3585
PubMed: 22499059
DOI: 10.1002/PROT.24094
Page generated: Fri Jul 11 11:44:03 2025

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