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Potassium in PDB 3b0n: Q448K Mutant of Assimilatory Nitrite Reductase (NII3) From Tobbaco Leaf

Enzymatic activity of Q448K Mutant of Assimilatory Nitrite Reductase (NII3) From Tobbaco Leaf

All present enzymatic activity of Q448K Mutant of Assimilatory Nitrite Reductase (NII3) From Tobbaco Leaf:
1.7.7.1;

Protein crystallography data

The structure of Q448K Mutant of Assimilatory Nitrite Reductase (NII3) From Tobbaco Leaf, PDB code: 3b0n 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) 30.66 / 2.00
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 133.455, 133.455, 77.656, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 18.6

Other elements in 3b0n:

The structure of Q448K Mutant of Assimilatory Nitrite Reductase (NII3) From Tobbaco Leaf 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 Q448K Mutant of Assimilatory Nitrite Reductase (NII3) From Tobbaco Leaf (pdb code 3b0n). 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 Q448K Mutant of Assimilatory Nitrite Reductase (NII3) From Tobbaco Leaf, PDB code: 3b0n:

Potassium binding site 1 out of 1 in 3b0n

Go back to Potassium Binding Sites List in 3b0n
Potassium binding site 1 out of 1 in the Q448K Mutant of Assimilatory Nitrite Reductase (NII3) From Tobbaco Leaf


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Q448K Mutant of Assimilatory Nitrite Reductase (NII3) From Tobbaco Leaf within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K603

b:22.8
occ:1.00
 OD1 A:ASN403 2.5 16.7 1.0
O A:HOH1013 2.6 19.1 1.0
O A:ILE371 2.6 14.4 1.0
O A:HOH1027 2.6 22.6 1.0
O A:GLU401 2.8 14.7 1.0
O A:GLN402 2.9 14.6 1.0
O A:HOH1042 3.3 16.6 1.0
CG A:ASN403 3.3 16.8 1.0
C A:GLN402 3.5 14.5 1.0
C A:ILE371 3.7 14.0 1.0
ND2 A:ASN403 3.8 13.2 1.0
O A:LEU437 3.9 18.3 1.0
N A:GLY374 3.9 15.0 1.0
C A:GLU401 4.0 14.5 1.0
N A:VAL373 4.0 15.0 1.0
CB A:GLN402 4.0 13.9 1.0
ND1 A:HIS370 4.1 16.8 1.0
N A:ASN403 4.1 14.8 1.0
N A:ILE371 4.2 13.4 1.0
CE1 A:HIS370 4.2 14.8 1.0
CA A:GLN402 4.2 13.9 1.0
CA A:ASN403 4.4 15.3 1.0
CA A:ILE371 4.4 13.8 1.0
CA A:VAL373 4.4 14.8 1.0
CB A:ASN403 4.5 15.0 1.0
N A:GLN402 4.5 14.3 1.0
C A:PRO372 4.6 14.2 1.0
CB A:ILE371 4.6 13.8 1.0
C A:VAL373 4.6 15.1 1.0
N A:PRO372 4.6 13.6 1.0
CA A:GLY374 4.7 15.5 1.0
CA A:PRO372 4.7 14.0 1.0
OE1 A:GLN402 4.8 15.2 1.0

Reference:

S.Nakano, M.Takahashi, A.Sakamoto, H.Morikawa, K.Katayanagi. Structure-Function Relationship of Assimilatory Nitrite Reductases From the Leaf and Root of Tobacco Based on High Resolution Structures Protein Sci. V. 21 383 2012.
ISSN: ISSN 0961-8368
PubMed: 22238192
DOI: 10.1002/PRO.2025
Page generated: Sat Aug 9 04:32:11 2025

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