Magnesium in PDB 4bix: Crystal Structure of Cpxahdc (Monoclinic Form 1)

All present enzymatic activity of Crystal Structure of Cpxahdc (Monoclinic Form 1):
2.7.13.3;

The structure of Crystal Structure of Cpxahdc (Monoclinic Form 1), PDB code: 4bix was solved by A.E.Mechaly, N.Sassoon, J.M.Betton, P.M.Alzari, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.54 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	95.186, 141.800, 55.214, 90.00, 94.33, 90.00
R / Rfree (%)	19.49 / 21.61

The binding sites of Magnesium atom in the Crystal Structure of Cpxahdc (Monoclinic Form 1) (pdb code 4bix). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Cpxahdc (Monoclinic Form 1), PDB code: 4bix:

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


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 (Monoclinic Form 1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1457 b:73.5 occ:1.00 NH1 A:ARG363 2.6 0.9 1.0 O3A A:ADP501 2.8 53.3 1.0 OH A:TYR364 2.9 63.9 1.0 OD1 A:ASN360 3.0 51.0 1.0 O1B A:ADP501 3.1 55.3 1.0 PB A:ADP501 3.4 55.5 1.0 CE2 A:TYR364 3.4 51.6 1.0 CZ A:TYR364 3.6 60.8 1.0 OG1 A:THR417 3.7 87.9 1.0 CZ A:ARG363 3.9 0.5 1.0 O3B A:ADP501 3.9 56.8 1.0 PA A:ADP501 3.9 46.4 1.0 C3' A:ADP501 3.9 49.0 1.0 CG A:ASN360 4.0 59.8 1.0 O1A A:ADP501 4.0 47.5 1.0 O3' A:ADP501 4.1 47.5 1.0 CD A:ARG363 4.2 86.6 1.0 O5' A:ADP501 4.2 48.2 1.0 NE A:ARG363 4.4 0.2 1.0 ND2 A:ASN360 4.5 49.4 1.0 CG2 A:THR417 4.6 87.8 1.0 CD2 A:TYR364 4.7 52.0 1.0 CB A:THR417 4.8 89.2 1.0 O A:HOH2102 4.8 61.3 1.0 C2' A:ADP501 4.8 50.4 1.0 NH2 A:ARG363 4.8 0.7 1.0 O2B A:ADP501 4.9 51.6 1.0 CE1 A:TYR364 5.0 55.1 1.0

A.E.Mechaly, N.Sassoon, J.M.Betton, P.M.Alzari. Segmental Helical Motions and Dynamical Asymmetry Modulate Histidine Kinase Autophosphorylation. Plos Biol. V. 12 1776 2014.
ISSN: ISSN 1544-9173
PubMed: 24492262
DOI: 10.1371/JOURNAL.PBIO.1001776