Magnesium in PDB 5lfk: Crystal Structure of Cpxahdc (Hemiphosphorylated Form)

All present enzymatic activity of Crystal Structure of Cpxahdc (Hemiphosphorylated Form):
2.7.13.3;

The structure of Crystal Structure of Cpxahdc (Hemiphosphorylated Form), PDB code: 5lfk was solved by A.E.Mechaly, P.M.Alzari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.70 / 3.09
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	145.734, 145.734, 225.191, 90.00, 90.00, 120.00
R / Rfree (%)	19.5 / 22

The binding sites of Magnesium atom in the Crystal Structure of Cpxahdc (Hemiphosphorylated Form) (pdb code 5lfk). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Cpxahdc (Hemiphosphorylated Form), PDB code: 5lfk:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Cpxahdc (Hemiphosphorylated Form)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Cpxahdc (Hemiphosphorylated Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg504 b:92.9 occ:1.00 O3G A:ATP503 2.8 0.2 1.0 O1A A:ATP503 2.9 73.1 1.0 ND2 A:ASN360 3.1 0.5 1.0 OD1 A:ASN356 3.2 0.8 1.0 OD1 A:ASN360 3.5 0.2 1.0 CG A:ASN360 3.7 0.1 1.0 CA A:GLY420 3.9 84.1 1.0 CG A:ASN356 3.9 0.7 1.0 CB A:ASN356 4.0 0.8 1.0 O1B A:ATP503 4.0 0.1 1.0 PG A:ATP503 4.3 0.8 1.0 C A:GLY420 4.3 78.3 1.0 O A:ASN356 4.3 98.8 1.0 PA A:ATP503 4.4 86.0 1.0 N A:LEU421 4.5 80.9 1.0 O2G A:ATP503 4.7 0.3 1.0 CA A:ASN356 4.7 95.0 1.0 C A:ASN356 4.7 93.8 1.0 N A:GLY420 4.8 85.9 1.0 O3A A:ATP503 4.9 93.0 1.0 PB A:ATP503 4.9 96.9 1.0 O A:GLY420 4.9 72.3 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Cpxahdc (Hemiphosphorylated Form)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Cpxahdc (Hemiphosphorylated Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:77.1 occ:1.00 OD1 B:ASN360 2.2 0.2 1.0 O3G B:ATP501 2.7 0.1 1.0 O2A B:ATP501 2.9 84.0 1.0 OD1 B:ASN356 3.1 91.3 1.0 CG B:ASN360 3.3 0.3 1.0 O2B B:ATP501 3.5 95.0 1.0 O1G B:ATP501 3.6 91.9 1.0 PG B:ATP501 3.7 95.7 1.0 ND2 B:ASN360 3.9 0.5 1.0 CA B:GLY420 3.9 90.6 1.0 O B:ASN356 3.9 80.3 1.0 CG B:ASN356 4.2 86.8 1.0 PA B:ATP501 4.3 90.6 1.0 CE1 A:HIS248 4.4 96.2 1.0 PB B:ATP501 4.4 91.5 1.0 NE2 A:HIS248 4.5 0.4 1.0 O3B B:ATP501 4.6 90.3 1.0 CB B:ASN360 4.6 0.5 1.0 CB B:ASN356 4.6 77.7 1.0 O3A B:ATP501 4.6 92.8 1.0 N B:ASN360 4.6 78.8 1.0 C B:ASN356 4.7 80.3 1.0 CA B:ASN356 4.7 74.3 1.0 N B:GLY420 4.7 0.5 1.0 CA B:ASN360 4.8 91.5 1.0 C B:GLY420 4.8 89.2 1.0 O2G B:ATP501 5.0 94.6 1.0

A.E.Mechaly, S.Soto Diaz, N.Sassoon, A.Buschiazzo, J.M.Betton, P.M.Alzari. Structural Coupling Between Autokinase and Phosphotransferase Reactions in A Bacterial Histidine Kinase. Structure V. 25 939 2017.
ISSN: ISSN 1878-4186
PubMed: 28552574
DOI: 10.1016/J.STR.2017.04.011