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Potassium in PDB 1mc5: Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh

Enzymatic activity of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh

All present enzymatic activity of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh:
1.1.1.1; 1.2.1.1;

Protein crystallography data

The structure of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh, PDB code: 1mc5 was solved by P.C.Sanghani, 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) 48.83 / 2.60
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.656, 78.656, 311.428, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 24.9

Other elements in 1mc5:

The structure of Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh 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 S-(Hydroxymethyl)Glutathione and Nadh (pdb code 1mc5). 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 Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh, PDB code: 1mc5:

Potassium binding site 1 out of 1 in 1mc5

Go back to Potassium Binding Sites List in 1mc5
Potassium binding site 1 out of 1 in the Ternary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with S-(Hydroxymethyl)Glutathione and Nadh


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 S-(Hydroxymethyl)Glutathione and Nadh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K400

b:38.1
occ:1.00
 O A:ALA186 2.8 18.8 1.0
OH A:TYR263 2.9 22.9 1.0
O A:HOH608 2.9 15.1 1.0
O A:LYS187 2.9 21.4 1.0
OE2 A:GLU189 2.9 28.1 1.0
C A:LYS187 3.6 22.4 1.0
O A:HOH503 3.7 11.1 1.0
O A:HOH627 3.8 44.7 1.0
CB A:LYS187 3.8 24.1 1.0
CD A:GLU189 3.8 26.2 1.0
CZ A:TYR263 3.9 26.3 1.0
C A:ALA186 4.0 22.6 1.0
CE2 A:TYR263 4.2 25.9 1.0
CA A:LYS187 4.3 22.2 1.0
OE1 A:GLU189 4.3 27.1 1.0
NZ B:LYS106 4.3 25.1 1.0
O B:HOH572 4.3 15.7 1.0
N A:LEU188 4.4 23.9 1.0
O A:HOH674 4.5 38.2 1.0
CA A:LEU188 4.6 25.6 1.0
N A:LYS187 4.6 22.5 1.0
CG A:GLU189 4.9 27.2 1.0

Reference:

P.C.Sanghani, W.F.Bosron, T.D.Hurley. Human Glutathione-Dependent Formaldehyde Dehydrogenase. Structural Changes Associated with Ternary Complex Formation Biochemistry V. 41 15189 2002.
ISSN: ISSN 0006-2960
PubMed: 12484756
DOI: 10.1021/BI026705Q
Page generated: Mon Aug 12 04:57:11 2024

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