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Potassium in PDB 2fzw: Structure of the Binary Complex of the E67L Mutant of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H)

Enzymatic activity of Structure of the Binary Complex of the E67L Mutant of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H)

All present enzymatic activity of Structure of the Binary Complex of the E67L Mutant of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H):
1.1.1.1; 1.1.1.284;

Protein crystallography data

The structure of Structure of the Binary Complex of the E67L Mutant of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H), PDB code: 2fzw was solved by P.C.Sanghani, H.Robinson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.84
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 79.270, 79.270, 311.680, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.4

Other elements in 2fzw:

The structure of Structure of the Binary Complex of the E67L Mutant of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H) also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of the Binary Complex of the E67L Mutant of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H) (pdb code 2fzw). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of the Binary Complex of the E67L Mutant of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H), PDB code: 2fzw:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 2fzw

Go back to Potassium Binding Sites List in 2fzw
Potassium binding site 1 out of 2 in the Structure of the Binary Complex of the E67L Mutant of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of the Binary Complex of the E67L Mutant of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1804

b:13.2
occ:1.00
 OH A:TYR263 2.9 11.3 1.0
O A:ALA186 3.0 13.8 1.0
O A:LYS187 3.1 15.4 1.0
OE2 A:GLU189 3.2 17.7 1.0
O B:HOH2859 3.2 21.4 1.0
O B:HOH2860 3.3 40.6 1.0
O B:HOH2875 3.4 43.6 1.0
C A:LYS187 3.7 14.9 1.0
CD A:GLU189 3.7 16.9 1.0
CB A:LYS187 3.9 18.3 1.0
O A:HOH1816 3.9 14.6 1.0
OE1 A:GLU189 3.9 13.9 1.0
CZ A:TYR263 4.0 10.6 1.0
C A:ALA186 4.1 14.5 1.0
CE2 A:TYR263 4.2 10.7 1.0
CA A:LYS187 4.3 15.4 1.0
NZ B:LYS106 4.3 13.5 1.0
N A:LEU188 4.4 15.7 1.0
O B:HOH2387 4.4 13.9 1.0
O A:HOH1931 4.5 24.6 1.0
CA A:LEU188 4.6 15.7 1.0
O A:HOH1910 4.6 24.9 1.0
N A:LYS187 4.7 13.8 1.0
CG A:GLU189 4.7 16.1 1.0

Potassium binding site 2 out of 2 in 2fzw

Go back to Potassium Binding Sites List in 2fzw
Potassium binding site 2 out of 2 in the Structure of the Binary Complex of the E67L Mutant of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of the Binary Complex of the E67L Mutant of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K1805

b:14.1
occ:1.00
 OH B:TYR263 2.9 12.5 1.0
O B:ALA186 2.9 15.3 1.0
O B:LYS187 3.0 15.7 1.0
OE2 B:GLU189 3.2 20.0 1.0
O B:HOH2732 3.2 18.9 1.0
O B:HOH2898 3.2 33.4 1.0
O B:HOH2741 3.3 35.8 1.0
O B:HOH2917 3.4 45.0 1.0
C B:LYS187 3.7 15.9 1.0
CD B:GLU189 3.8 21.3 1.0
CB B:LYS187 3.9 16.8 1.0
CZ B:TYR263 3.9 13.8 1.0
O B:HOH2414 4.0 13.1 1.0
OE1 B:GLU189 4.0 18.8 1.0
C B:ALA186 4.1 14.1 1.0
CE2 B:TYR263 4.2 13.0 1.0
CA B:LYS187 4.3 15.6 1.0
NZ A:LYS106 4.3 17.8 1.0
O A:HOH1827 4.4 13.9 1.0
O B:HOH2575 4.4 29.1 1.0
N B:LEU188 4.4 16.2 1.0
O B:HOH2918 4.6 35.8 1.0
CA B:LEU188 4.6 16.7 1.0
N B:LYS187 4.7 14.4 1.0
O2 B:PO41801 4.8 64.5 1.0
CG B:GLU189 4.9 19.1 1.0

Reference:

P.C.Sanghani, W.I.Davis, L.Zhai, H.Robinson. Structure-Function Relationships in Human Glutathione-Dependent Formaldehyde Dehydrogenase. Role of Glu-67 and Arg-368 in the Catalytic Mechanism. Biochemistry V. 45 4819 2006.
ISSN: ISSN 0006-2960
PubMed: 16605250
DOI: 10.1021/BI052554Q
Page generated: Sat Aug 9 03:27:32 2025

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