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Potassium in PDB 1ma0: Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad+ and Dodecanoic Acid

Enzymatic activity of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad+ and Dodecanoic Acid

All present enzymatic activity of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad+ and Dodecanoic Acid:
1.1.1.1;

Protein crystallography data

The structure of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad+ and Dodecanoic Acid, PDB code: 1ma0 was solved by P.C.Sanghani, H.Robinson, W.F.Bosron, T.D.Hurley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.82 / 2.30
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.660, 78.660, 310.920, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 22.3

Other elements in 1ma0:

The structure of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad+ and Dodecanoic Acid also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad+ and Dodecanoic Acid (pdb code 1ma0). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad+ and Dodecanoic Acid, PDB code: 1ma0:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1ma0

Go back to Potassium Binding Sites List in 1ma0
Potassium binding site 1 out of 2 in the Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad+ and Dodecanoic Acid


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad+ and Dodecanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K6602

b:27.5
occ:1.00
O A:HOH6728 2.8 25.1 1.0
OH A:TYR263 2.9 23.1 1.0
O A:ALA186 2.9 22.1 1.0
O A:LYS187 3.0 24.1 1.0
OE2 A:GLU189 3.1 23.4 1.0
O A:HOH6762 3.2 41.1 1.0
C A:LYS187 3.7 24.7 1.0
O A:HOH6612 3.8 22.2 1.0
CD A:GLU189 3.8 23.6 1.0
CZ A:TYR263 3.8 22.2 1.0
CB A:LYS187 3.9 28.0 1.0
CE2 A:TYR263 4.1 21.2 1.0
C A:ALA186 4.1 23.9 1.0
OE1 A:GLU189 4.1 20.9 1.0
CA A:LYS187 4.3 25.9 1.0
O B:HOH6555 4.3 23.0 1.0
NZ B:LYS106 4.3 24.9 1.0
N A:LEU188 4.4 25.2 1.0
O A:HOH6794 4.5 48.8 1.0
O A:HOH6773 4.6 38.8 1.0
CA A:LEU188 4.6 26.5 1.0
N A:LYS187 4.7 24.9 1.0
O A:HOH6708 4.7 30.0 1.0
CG A:GLU189 4.9 22.8 1.0

Potassium binding site 2 out of 2 in 1ma0

Go back to Potassium Binding Sites List in 1ma0
Potassium binding site 2 out of 2 in the Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad+ and Dodecanoic Acid


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad+ and Dodecanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K6501

b:31.6
occ:1.00
O B:LYS187 2.8 24.7 1.0
O A:HOH6804 2.8 34.0 1.0
O B:ALA186 2.9 20.4 1.0
OH B:TYR263 2.9 18.2 1.0
OE2 B:GLU189 3.0 25.2 1.0
O B:HOH6684 3.0 27.1 1.0
O A:HOH6799 3.1 44.0 1.0
C B:LYS187 3.6 24.5 1.0
CB B:LYS187 3.7 25.7 1.0
CD B:GLU189 3.8 25.3 1.0
O B:HOH6516 3.9 21.9 1.0
CZ B:TYR263 3.9 20.8 1.0
C B:ALA186 4.0 21.2 1.0
OE1 B:GLU189 4.1 22.5 1.0
CA B:LYS187 4.2 24.7 1.0
O A:HOH6833 4.2 56.2 1.0
CE2 B:TYR263 4.2 21.0 1.0
NZ A:LYS106 4.3 25.1 1.0
N B:LEU188 4.4 25.6 1.0
O A:HOH6614 4.4 19.5 1.0
O B:HOH6740 4.5 43.4 1.0
N B:LYS187 4.6 22.9 1.0
CA B:LEU188 4.6 26.9 1.0
CG B:GLU189 4.9 25.6 1.0

Reference:

P.C.Sanghani, H.Robinson, W.F.Bosron, T.D.Hurley. Human Glutathione-Dependent Formaldehyde Dehydrogenase. Structures of Apo, Binary, and Inhibitory Ternary Complexes. Biochemistry V. 41 10778 2002.
ISSN: ISSN 0006-2960
PubMed: 12196016
DOI: 10.1021/BI0257639
Page generated: Mon Aug 12 04:56:49 2024

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