Magnesium in PDB 4hqu: Crystal Structure of Human Pdgf-Bb in Complex with A Modified Nucleotide Aptamer (Somamer SL5)

The structure of Crystal Structure of Human Pdgf-Bb in Complex with A Modified Nucleotide Aptamer (Somamer SL5), PDB code: 4hqu was solved by D.R.Davies, T.E.Edwards, N.Janjic, A.D.Gelinas, C.Zhang, T.C.Jarvis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.27 / 2.20
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	59.710, 59.710, 167.010, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 26.2

The structure of Crystal Structure of Human Pdgf-Bb in Complex with A Modified Nucleotide Aptamer (Somamer SL5) also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of Human Pdgf-Bb in Complex with A Modified Nucleotide Aptamer (Somamer SL5) (pdb code 4hqu). 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 Human Pdgf-Bb in Complex with A Modified Nucleotide Aptamer (Somamer SL5), PDB code: 4hqu:

Magnesium binding site 1 out of 1 in the Crystal Structure of Human Pdgf-Bb in Complex with A Modified Nucleotide Aptamer (Somamer SL5)


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 Human Pdgf-Bb in Complex with A Modified Nucleotide Aptamer (Somamer SL5) within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg102 b:33.9 occ:0.50 O C:HOH205 2.2 31.0 0.5 O C:HOH206 2.2 32.3 0.5 O C:HOH202 2.2 32.4 0.5 O C:HOH204 2.2 33.6 0.5 O C:HOH201 2.2 32.6 0.5 O C:HOH203 2.2 32.4 0.5 O6 C:18M24 4.2 47.5 1.0 O C:HOH227 4.2 37.1 1.0 OP1 C:A2M11 4.2 37.6 1.0 O C:HOH228 4.4 40.0 1.0 N7 C:A2M11 4.5 48.8 1.0 N4 C:DC12 4.7 45.3 1.0

D.R.Davies, A.D.Gelinas, C.Zhang, J.C.Rohloff, J.D.Carter, D.O'connell, S.M.Waugh, S.K.Wolk, W.S.Mayfield, A.B.Burgin, T.E.Edwards, L.J.Stewart, L.Gold, N.Janjic, T.C.Jarvis. Unique Motifs and Hydrophobic Interactions Shape the Binding of Modified Dna Ligands to Protein Targets. Proc.Natl.Acad.Sci.Usa V. 109 19971 2012.
ISSN: ISSN 0027-8424
PubMed: 23139410
DOI: 10.1073/PNAS.1213933109