Magnesium in PDB 1w5t: Structure of the Aeropyrum Pernix ORC2 Protein (Adpnp-Adp Complexes)

The structure of Structure of the Aeropyrum Pernix ORC2 Protein (Adpnp-Adp Complexes), PDB code: 1w5t was solved by M.R.Singleton, R.Morales, I.Grainge, N.Cook, M.N.Isupov, D.B.Wigley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.4
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	61.489, 61.489, 267.865, 90.00, 90.00, 120.00
R / Rfree (%)	21.1 / 27.9

The binding sites of Magnesium atom in the Structure of the Aeropyrum Pernix ORC2 Protein (Adpnp-Adp Complexes) (pdb code 1w5t). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Structure of the Aeropyrum Pernix ORC2 Protein (Adpnp-Adp Complexes), PDB code: 1w5t:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Structure of the Aeropyrum Pernix ORC2 Protein (Adpnp-Adp Complexes)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Aeropyrum Pernix ORC2 Protein (Adpnp-Adp Complexes) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg701 b:3.8 occ:1.00 O A:HOH2029 2.1 10.4 1.0 O1B A:ANP700 2.2 14.3 1.0 O A:HOH2063 2.2 4.8 1.0 OG1 A:THR66 2.3 12.5 1.0 O2G A:ANP700 2.3 17.6 1.0 PB A:ANP700 3.4 9.3 1.0 CB A:THR66 3.4 13.0 1.0 PG A:ANP700 3.6 13.7 1.0 N3B A:ANP700 3.7 11.1 1.0 N A:THR66 4.1 12.9 1.0 O2A A:ANP700 4.2 10.4 1.0 OD2 A:ASP145 4.2 13.0 1.0 O A:HOH2022 4.3 23.6 1.0 CA A:THR66 4.3 12.8 1.0 OD1 A:ASP145 4.4 15.2 1.0 O2B A:ANP700 4.4 12.1 1.0 CG2 A:THR66 4.4 10.0 1.0 OE1 A:GLU146 4.4 26.0 1.0 O1G A:ANP700 4.5 19.2 1.0 O3A A:ANP700 4.6 11.3 1.0 O A:HOH2031 4.6 17.5 1.0 CB A:LYS65 4.7 11.7 1.0 CE A:LYS65 4.7 14.2 1.0 O3G A:ANP700 4.7 13.2 1.0 CG A:ASP145 4.7 14.2 1.0 PA A:ANP700 4.8 8.1 1.0 NH1 A:ARG260 4.9 43.6 1.0

Magnesium binding site 2 out of 3 in the Structure of the Aeropyrum Pernix ORC2 Protein (Adpnp-Adp Complexes)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Aeropyrum Pernix ORC2 Protein (Adpnp-Adp Complexes) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg701 b:5.6 occ:1.00 O B:HOH2040 2.0 13.3 1.0 O1B B:ANP700 2.0 16.0 1.0 OG1 B:THR66 2.2 12.9 1.0 O2G B:ANP700 2.2 30.0 1.0 O B:HOH2014 2.3 7.4 1.0 O B:HOH2015 2.6 21.1 1.0 PB B:ANP700 3.4 13.4 1.0 CB B:THR66 3.4 12.8 1.0 PG B:ANP700 3.6 31.9 1.0 N3B B:ANP700 3.9 22.0 1.0 OD2 B:ASP145 4.0 12.9 1.0 N B:THR66 4.1 12.5 1.0 O2A B:ANP700 4.3 13.9 1.0 CA B:THR66 4.4 12.8 1.0 OE1 B:GLU146 4.4 25.4 1.0 O2B B:ANP700 4.4 16.9 1.0 CG2 B:THR66 4.4 10.1 1.0 OD1 B:ASP145 4.5 14.8 1.0 O1G B:ANP700 4.6 30.6 1.0 CE B:LYS65 4.6 14.0 1.0 O3A B:ANP700 4.6 14.5 1.0 CB B:LYS65 4.7 11.5 1.0 CG B:ASP145 4.7 14.2 1.0 O3G B:ANP700 4.8 32.3 1.0 PA B:ANP700 4.9 12.2 1.0 NH1 B:ARG260 5.0 43.7 1.0

Magnesium binding site 3 out of 3 in the Structure of the Aeropyrum Pernix ORC2 Protein (Adpnp-Adp Complexes)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of the Aeropyrum Pernix ORC2 Protein (Adpnp-Adp Complexes) within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg701 b:19.4 occ:1.00 O3B C:ADP700 2.2 21.4 1.0 OG1 C:THR66 2.4 19.5 1.0 PB C:ADP700 3.4 20.1 1.0 O1B C:ADP700 3.5 19.3 1.0 CB C:THR66 3.6 20.2 1.0 OE1 C:GLU146 3.8 27.2 1.0 OD2 C:ASP145 4.0 21.6 1.0 O2A C:ADP700 4.0 19.9 1.0 OD1 C:ASP145 4.1 16.3 1.0 N C:THR66 4.2 19.0 1.0 O2B C:ADP700 4.3 26.2 1.0 CE C:LYS65 4.5 19.8 1.0 CG C:ASP145 4.5 19.5 1.0 CA C:THR66 4.5 20.1 1.0 O3A C:ADP700 4.5 20.9 1.0 CG2 C:THR66 4.6 19.1 1.0 NZ C:LYS65 4.7 23.1 1.0 PA C:ADP700 4.8 21.5 1.0 CD C:GLU146 4.8 23.8 1.0 CB C:LYS65 4.9 16.8 1.0

M.R.Singleton, R.Morales, I.Grainge, N.Cook, M.N.Isupov, D.B.Wigley. Conformational Changes Induced By Nucleotide Binding in CDC6/Orc From Aeropyrum Pernix J.Mol.Biol. V. 343 547 2004.
ISSN: ISSN 0022-2836
PubMed: 15465044
DOI: 10.1016/J.JMB.2004.08.044