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Potassium in PDB 1m6w: Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase and 12-Hydroxydodecanoic Acid

Enzymatic activity of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase and 12-Hydroxydodecanoic Acid

All present enzymatic activity of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase and 12-Hydroxydodecanoic Acid:
1.1.1.1;

Protein crystallography data

The structure of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase and 12-Hydroxydodecanoic Acid, PDB code: 1m6w 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) 20.00 / 2.30
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.632, 78.632, 309.417, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 22.5

Other elements in 1m6w:

The structure of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase and 12-Hydroxydodecanoic Acid also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase and 12-Hydroxydodecanoic Acid (pdb code 1m6w). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase and 12-Hydroxydodecanoic Acid, PDB code: 1m6w:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 1m6w

Go back to Potassium Binding Sites List in 1m6w
Potassium binding site 1 out of 2 in the Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase and 12-Hydroxydodecanoic Acid


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase and 12-Hydroxydodecanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K2001

b:22.2
occ:1.00
OH A:TYR263 2.8 17.3 1.0
O A:LYS187 2.9 19.7 1.0
OE2 A:GLU189 2.9 16.5 1.0
O A:ALA186 2.9 16.8 1.0
O A:HOH4479 2.9 26.1 1.0
O A:HOH4422 3.1 27.2 1.0
O B:HOH5708 3.1 40.7 1.0
C A:LYS187 3.6 21.2 1.0
CD A:GLU189 3.6 17.1 1.0
CZ A:TYR263 3.8 15.4 1.0
CB A:LYS187 3.8 23.7 1.0
OE1 A:GLU189 3.9 14.9 1.0
O A:HOH4381 4.0 17.4 1.0
C A:ALA186 4.1 19.2 1.0
CE2 A:TYR263 4.1 14.0 1.0
NZ B:LYS106 4.2 18.3 1.0
CA A:LYS187 4.3 21.6 1.0
N A:LEU188 4.3 20.9 1.0
O B:HOH5397 4.4 15.1 1.0
CA A:LEU188 4.5 21.4 1.0
O A:HOH4552 4.6 25.1 1.0
O A:HOH4506 4.6 34.6 1.0
N A:LYS187 4.7 19.7 1.0
CG A:GLU189 4.7 16.8 1.0
CE1 A:TYR263 5.0 14.4 1.0

Potassium binding site 2 out of 2 in 1m6w

Go back to Potassium Binding Sites List in 1m6w
Potassium binding site 2 out of 2 in the Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase and 12-Hydroxydodecanoic Acid


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase and 12-Hydroxydodecanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K2002

b:23.3
occ:1.00
OH B:TYR263 2.7 16.6 1.0
O B:LYS187 2.8 21.0 1.0
O B:ALA186 2.9 18.8 1.0
O B:HOH5580 2.9 33.0 1.0
OE2 B:GLU189 2.9 23.8 1.0
O B:HOH5660 3.0 33.2 1.0
O B:HOH5520 3.0 18.4 1.0
C B:LYS187 3.6 21.1 1.0
CD B:GLU189 3.7 21.9 1.0
CZ B:TYR263 3.8 17.6 1.0
CB B:LYS187 3.9 24.3 1.0
OE1 B:GLU189 3.9 22.3 1.0
C B:ALA186 4.0 19.6 1.0
O B:HOH5399 4.1 19.3 1.0
NZ A:LYS106 4.1 16.8 1.0
CE2 B:TYR263 4.1 15.8 1.0
O A:HOH4442 4.3 12.8 1.0
CA B:LYS187 4.3 21.7 1.0
N B:LEU188 4.4 19.7 1.0
O B:HOH5500 4.5 31.7 1.0
CA B:LEU188 4.5 21.1 1.0
O A:HOH4560 4.5 31.7 1.0
N B:LYS187 4.6 20.0 1.0
CG B:GLU189 4.8 21.8 1.0
CE1 B:TYR263 4.9 17.0 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 04:56:06 2024

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