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Potassium in PDB 3vks: Assimilatory Nitrite Reductase (NII3) - No Complex From Tobbaco Leaf

Enzymatic activity of Assimilatory Nitrite Reductase (NII3) - No Complex From Tobbaco Leaf

All present enzymatic activity of Assimilatory Nitrite Reductase (NII3) - No Complex From Tobbaco Leaf:
1.7.7.1;

Protein crystallography data

The structure of Assimilatory Nitrite Reductase (NII3) - No Complex From Tobbaco Leaf, PDB code: 3vks 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) 23.49 / 1.40
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 132.758, 132.758, 77.539, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 16.8

Other elements in 3vks:

The structure of Assimilatory Nitrite Reductase (NII3) - No Complex 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 Assimilatory Nitrite Reductase (NII3) - No Complex From Tobbaco Leaf (pdb code 3vks). 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) - No Complex From Tobbaco Leaf, PDB code: 3vks:

Potassium binding site 1 out of 1 in 3vks

Go back to Potassium Binding Sites List in 3vks
Potassium binding site 1 out of 1 in the Assimilatory Nitrite Reductase (NII3) - No Complex 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 Assimilatory Nitrite Reductase (NII3) - No Complex From Tobbaco Leaf within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K603

b:10.5
occ:1.00
 O A:HOH1013 2.7 11.2 1.0
O A:ILE371 2.7 9.9 1.0
OD1 A:ASN403 2.7 9.9 1.0
O A:HOH1027 2.8 12.5 1.0
O A:GLU401 2.9 10.4 1.0
O A:GLN402 2.9 10.0 1.0
O A:HOH1042 3.0 11.2 1.0
CG A:ASN403 3.4 9.8 1.0
C A:GLN402 3.4 9.6 1.0
C A:ILE371 3.8 10.0 1.0
O A:LEU437 3.8 11.3 1.0
ND2 A:ASN403 3.8 10.8 1.0
CB A:GLN402 3.9 9.6 1.0
N A:GLY374 4.0 9.7 1.0
C A:GLU401 4.0 9.8 1.0
N A:VAL373 4.0 10.4 1.0
ND1 A:HIS370 4.0 12.7 1.0
N A:ASN403 4.1 9.3 1.0
CA A:GLN402 4.1 9.4 1.0
CE1 A:HIS370 4.1 8.9 1.0
N A:ILE371 4.2 9.7 1.0
CA A:VAL373 4.4 10.7 1.0
CA A:ASN403 4.4 9.6 1.0
CA A:ILE371 4.5 9.9 1.0
CB A:ASN403 4.5 9.6 1.0
N A:GLN402 4.5 9.6 1.0
C A:VAL373 4.6 10.5 1.0
C A:PRO372 4.6 10.2 1.0
CA A:GLY374 4.7 10.4 1.0
N A:PRO372 4.7 9.9 1.0
CB A:ILE371 4.7 9.6 1.0
CA A:PRO372 4.8 10.2 1.0
OE1 A:GLN402 4.8 10.1 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 09:49:12 2024

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