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Potassium in PDB 3vkr: Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with High X-Ray Dose

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

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

Protein crystallography data

The structure of Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with High X-Ray Dose, PDB code: 3vkr 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) 37.22 / 1.60
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 134.165, 134.165, 78.002, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / 16.5

Other elements in 3vkr:

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

Iron (Fe) 5 atoms
Chlorine (Cl) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with High X-Ray Dose (pdb code 3vkr). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with High X-Ray Dose, PDB code: 3vkr:

Potassium binding site 1 out of 1 in 3vkr

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


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Assimilatory Nitrite Reductase (NII3) - NO2 Complex From Tobbaco Leaf Analysed with High X-Ray Dose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K603

b:7.4
occ:1.00
 O A:HOH1013 2.6 7.8 1.0
O A:ILE371 2.7 7.1 1.0
OD1 A:ASN403 2.7 6.3 1.0
O A:HOH1027 2.8 9.2 1.0
O A:GLU401 2.9 6.4 1.0
O A:GLN402 2.9 6.7 1.0
O A:HOH1042 3.0 9.4 1.0
CG A:ASN403 3.4 6.8 1.0
C A:GLN402 3.4 6.4 1.0
C A:ILE371 3.8 6.9 1.0
ND2 A:ASN403 3.8 7.7 1.0
O A:LEU437 3.8 8.0 1.0
N A:GLY374 3.9 6.9 1.0
CB A:GLN402 3.9 6.1 1.0
C A:GLU401 4.0 6.1 1.0
N A:VAL373 4.0 6.8 1.0
ND1 A:HIS370 4.1 9.7 1.0
N A:ASN403 4.1 6.1 1.0
CA A:GLN402 4.1 5.8 1.0
CE1 A:HIS370 4.1 4.9 1.0
N A:ILE371 4.3 6.4 1.0
CA A:VAL373 4.4 7.3 1.0
CA A:ASN403 4.5 6.3 1.0
CA A:ILE371 4.5 6.7 1.0
N A:GLN402 4.5 5.5 1.0
CB A:ASN403 4.5 6.9 1.0
C A:VAL373 4.6 7.3 1.0
C A:PRO372 4.6 6.7 1.0
CA A:GLY374 4.7 7.4 1.0
N A:PRO372 4.7 7.2 1.0
CB A:ILE371 4.7 6.8 1.0
CA A:PRO372 4.7 7.0 1.0
OE1 A:GLN402 4.8 7.2 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: Mon Aug 12 09:49:11 2024

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