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Potassium in PDB 3vm1: Assimilatory Nitrite Reductase (NII3) - N226K Mutant - HCO3 Complex From Tobacco Leaf

Enzymatic activity of Assimilatory Nitrite Reductase (NII3) - N226K Mutant - HCO3 Complex From Tobacco Leaf

All present enzymatic activity of Assimilatory Nitrite Reductase (NII3) - N226K Mutant - HCO3 Complex From Tobacco Leaf:
1.7.7.1;

Protein crystallography data

The structure of Assimilatory Nitrite Reductase (NII3) - N226K Mutant - HCO3 Complex From Tobacco Leaf, PDB code: 3vm1 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) 35.94 / 1.50
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 133.616, 133.616, 77.742, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 17.9

Other elements in 3vm1:

The structure of Assimilatory Nitrite Reductase (NII3) - N226K Mutant - HCO3 Complex From Tobacco 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) - N226K Mutant - HCO3 Complex From Tobacco Leaf (pdb code 3vm1). 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) - N226K Mutant - HCO3 Complex From Tobacco Leaf, PDB code: 3vm1:

Potassium binding site 1 out of 1 in 3vm1

Go back to Potassium Binding Sites List in 3vm1
Potassium binding site 1 out of 1 in the Assimilatory Nitrite Reductase (NII3) - N226K Mutant - HCO3 Complex From Tobacco 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) - N226K Mutant - HCO3 Complex From Tobacco Leaf within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K603

b:9.2
occ:1.00
 O A:HOH1013 2.5 10.5 1.0
OD1 A:ASN403 2.6 7.0 1.0
O A:ILE371 2.6 6.9 1.0
O A:HOH1027 2.7 11.1 1.0
O A:GLU401 2.8 6.6 1.0
O A:GLN402 2.9 6.2 1.0
O A:HOH1042 3.1 9.0 1.0
CG A:ASN403 3.4 7.2 1.0
C A:GLN402 3.4 6.2 1.0
C A:ILE371 3.7 6.6 1.0
ND2 A:ASN403 3.8 7.2 1.0
O A:LEU437 3.8 9.2 1.0
CB A:GLN402 3.9 6.5 1.0
N A:GLY374 4.0 6.7 1.0
C A:GLU401 4.0 6.3 1.0
N A:VAL373 4.0 7.1 1.0
N A:ASN403 4.0 6.1 1.0
ND1 A:HIS370 4.0 10.5 1.0
CA A:GLN402 4.1 6.2 1.0
CE1 A:HIS370 4.2 5.5 1.0
N A:ILE371 4.2 6.9 1.0
CA A:VAL373 4.4 7.5 1.0
CA A:ASN403 4.4 6.3 1.0
CA A:ILE371 4.4 7.1 1.0
CB A:ASN403 4.5 6.6 1.0
N A:GLN402 4.5 6.3 1.0
C A:PRO372 4.6 6.9 1.0
C A:VAL373 4.6 7.3 1.0
CB A:ILE371 4.7 7.2 1.0
N A:PRO372 4.7 6.9 1.0
CA A:GLY374 4.7 7.0 1.0
CA A:PRO372 4.7 6.7 1.0
OE1 A:GLN402 4.8 7.7 1.0

Reference:

S.Nakano, M.Takahashi, A.Sakamoto, H.Morikawa, K.Katayanagi. X-Ray Crystal Structure of A Mutant Assimilatory Nitrite Reductase That Shows Sulfite Reductase-Like Activity Chem.Biodivers. V. 9 1989 2012.
ISSN: ISSN 1612-1872
PubMed: 22976986
DOI: 10.1002/CBDV.201100442
Page generated: Mon Aug 12 09:49:43 2024

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