Potassium in PDB 7ruv: Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin

Enzymatic activity of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin

All present enzymatic activity of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin:
2.5.1.17;

Protein crystallography data

The structure of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin, PDB code: 7ruv was solved by R.Mascarenhas, H.Gouda, M.Koutmos, R.Banerjee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.00 / 2.10
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 121.181, 121.181, 169.77, 90, 90, 120
R / Rfree (%) 18.5 / 21.7

Other elements in 7ruv:

The structure of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin also contains other interesting chemical elements:

Cobalt (Co) 4 atoms
Magnesium (Mg) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin (pdb code 7ruv). 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 Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin, PDB code: 7ruv:

Potassium binding site 1 out of 1 in 7ruv

Go back to Potassium Binding Sites List in 7ruv
Potassium binding site 1 out of 1 in the Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Human Atp:Cobalamin Adenosyltransferase E193K Bound to Adenosylcobalamin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K301

b:46.1
occ:0.33
 NH1 A:ARG195 3.3 36.5 1.0
O A:HOH416 3.3 37.7 1.0
CD A:ARG191 4.0 36.6 1.0
OE2 A:GLU84 4.3 45.8 1.0
CZ A:ARG195 4.4 45.0 1.0
NH2 A:ARG191 4.5 35.9 1.0
NE A:ARG191 4.5 35.0 1.0
NE A:ARG195 4.7 41.6 1.0
CZ A:ARG191 4.8 40.2 1.0
O A:HOH436 4.9 63.0 0.3

Reference:

H.Gouda, R.Mascarenhas, S.Pillay, M.Ruetz, M.Koutmos, R.Banerjee. Patient Mutations in Human Atp:Cob(I)Alamin Adenosyltransferase Differentially Affect Its Catalytic Versus Chaperone Functions. J.Biol.Chem. 01373 2021.
ISSN: ESSN 1083-351X
PubMed: 34757128
DOI: 10.1016/J.JBC.2021.101373
Page generated: Mon Aug 12 20:57:15 2024

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