Magnesium in PDB 4ohv: Structure of A Rna-Processing Protein

The structure of Structure of A Rna-Processing Protein, PDB code: 4ohv was solved by A.Dikfidan, B.Loll, C.Zeymer, T.Clausen, A.Meinhart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	87.23 / 2.30
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	100.720, 100.720, 40.380, 90.00, 90.00, 120.00
R / Rfree (%)	19.2 / 24

The binding sites of Magnesium atom in the Structure of A Rna-Processing Protein (pdb code 4ohv). 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 Structure of A Rna-Processing Protein, PDB code: 4ohv:

Magnesium binding site 1 out of 1 in the Structure of A Rna-Processing Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of A Rna-Processing Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:32.3 occ:1.00 O2B A:ANP501 1.9 29.1 1.0 O1G A:ANP501 2.0 31.4 1.0 O A:HOH601 2.0 25.0 1.0 O A:HOH603 2.0 27.3 1.0 O A:HOH602 2.2 27.1 1.0 OG1 A:THR128 2.3 20.0 1.0 PB A:ANP501 3.1 28.5 1.0 PG A:ANP501 3.1 32.4 1.0 CB A:THR128 3.3 21.7 1.0 N3B A:ANP501 3.3 29.8 1.0 N A:THR128 3.8 20.8 1.0 O1A A:ANP501 3.9 29.8 1.0 O A:HOH612 3.9 48.5 1.0 O3G A:ANP501 4.0 34.1 1.0 O1B A:ANP501 4.0 30.0 1.0 OD2 A:ASP151 4.1 30.7 1.0 CA A:THR128 4.1 20.1 1.0 ND2 A:ASN229 4.1 28.9 1.0 O2G A:ANP501 4.3 32.2 1.0 O3A A:ANP501 4.3 28.7 1.0 OD1 A:ASN229 4.3 29.7 1.0 CG2 A:THR128 4.5 20.5 1.0 O A:HOH611 4.5 36.8 1.0 PA A:ANP501 4.6 29.8 1.0 CB A:LYS127 4.7 22.7 1.0 CG A:ASN229 4.7 25.8 1.0 O A:HOH604 4.8 30.0 1.0 C A:LYS127 4.9 20.4 1.0 O A:GLN154 4.9 31.5 1.0 O2A A:ANP501 5.0 27.9 1.0

A.Dikfidan, B.Loll, C.Zeymer, I.Magler, T.Clausen, A.Meinhart. Rna Specificity and Regulation of Catalysis in the Eukaryotic Polynucleotide Kinase CLP1. Mol.Cell V. 54 975 2014.
ISSN: ISSN 1097-2765
PubMed: 24813946
DOI: 10.1016/J.MOLCEL.2014.04.005