Magnesium in PDB 1id0: Crystal Structure of the Nucleotide Bond Conformation of Phoq Kinase Domain

All present enzymatic activity of Crystal Structure of the Nucleotide Bond Conformation of Phoq Kinase Domain:
2.7.1.37;

The structure of Crystal Structure of the Nucleotide Bond Conformation of Phoq Kinase Domain, PDB code: 1id0 was solved by A.Marina, C.Mott, A.Auyzenberg, C.D.Waldburger, W.A.Hendrickson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.50 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.503, 45.004, 71.764, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 23.3

The binding sites of Magnesium atom in the Crystal Structure of the Nucleotide Bond Conformation of Phoq Kinase Domain (pdb code 1id0). 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 the Nucleotide Bond Conformation of Phoq Kinase Domain, PDB code: 1id0:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Nucleotide Bond Conformation of Phoq Kinase Domain


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 the Nucleotide Bond Conformation of Phoq Kinase Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg700 b:24.4 occ:1.00 O A:HOH84 2.3 24.2 1.0 OD1 A:ASN385 2.3 19.5 1.0 O2B A:ANP487 2.4 28.2 1.0 OE1 A:GLN442 2.5 32.5 1.0 O2G A:ANP487 2.5 28.4 1.0 O2A A:ANP487 2.8 17.4 1.0 CG A:ASN385 3.2 18.3 1.0 PB A:ANP487 3.4 30.2 1.0 CD A:GLN442 3.5 33.4 1.0 ND2 A:ASN385 3.5 16.5 1.0 O3A A:ANP487 3.7 20.6 1.0 PG A:ANP487 3.8 27.1 1.0 ND2 A:ASN389 3.8 14.0 1.0 PA A:ANP487 3.8 17.2 1.0 N3B A:ANP487 3.9 23.5 1.0 NE2 A:GLN442 4.1 35.8 1.0 N A:GLY443 4.1 24.2 1.0 OD1 A:ASN389 4.1 17.1 1.0 CA A:GLY445 4.1 16.0 1.0 N A:GLY445 4.2 17.0 1.0 NH2 A:ARG434 4.2 26.4 1.0 CG A:ASN389 4.3 15.6 1.0 O A:HOH154 4.4 38.8 1.0 O A:ASN385 4.4 11.1 1.0 CA A:GLY443 4.5 21.4 1.0 CB A:ASN385 4.5 12.9 1.0 O3G A:ANP487 4.5 27.9 1.0 OD1 A:ASP388 4.6 25.4 1.0 C A:GLY443 4.6 20.7 1.0 O A:GLY443 4.6 21.9 1.0 O1A A:ANP487 4.6 18.8 1.0 O1B A:ANP487 4.7 27.6 1.0 CG A:GLN442 4.7 32.8 1.0 O1G A:ANP487 4.8 29.0 1.0 CA A:ASN385 4.8 12.2 1.0

A.Marina, C.Mott, A.Auyzenberg, W.A.Hendrickson, C.D.Waldburger. Structural and Mutational Analysis of the Phoq Histidine Kinase Catalytic Domain. Insight Into the Reaction Mechanism. J.Biol.Chem. V. 276 41182 2001.
ISSN: ISSN 0021-9258
PubMed: 11493605
DOI: 10.1074/JBC.M106080200