Magnesium in PDB 2vhu: P4 Protein From Bacteriophage PHI12 K241C Mutant in Complex with Adp and Mgcl

The structure of P4 Protein From Bacteriophage PHI12 K241C Mutant in Complex with Adp and Mgcl, PDB code: 2vhu was solved by D.E.Kainov, E.J.Mancini, J.Telenius, J.Lisal, J.M.Grimes, D.H.Bamford, D.I.Stuart, R.Tuma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	100.00 / 2.75
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	105.301, 128.485, 158.562, 90.00, 90.00, 90.00
R / Rfree (%)	21.9 / 28.4

The binding sites of Magnesium atom in the P4 Protein From Bacteriophage PHI12 K241C Mutant in Complex with Adp and Mgcl (pdb code 2vhu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the P4 Protein From Bacteriophage PHI12 K241C Mutant in Complex with Adp and Mgcl, PDB code: 2vhu:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the P4 Protein From Bacteriophage PHI12 K241C Mutant in Complex with Adp and Mgcl


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of P4 Protein From Bacteriophage PHI12 K241C Mutant in Complex with Adp and Mgcl within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1302 b:59.6 occ:1.00 OG1 A:THR137 2.3 34.7 1.0 O2B A:ADP1301 2.7 68.1 1.0 O2A A:ADP1301 2.8 67.0 1.0 OD1 A:ASP189 3.4 35.6 1.0 OG A:SER232 3.4 48.9 1.0 O1B A:ADP1301 3.4 67.5 1.0 PB A:ADP1301 3.5 67.9 1.0 CB A:THR137 3.6 34.2 1.0 ND2 A:ASN234 3.7 66.4 1.0 N A:THR137 3.8 35.6 1.0 PA A:ADP1301 4.0 68.0 1.0 O3A A:ADP1301 4.0 68.2 1.0 CA A:THR137 4.1 34.2 1.0 CG A:ASP189 4.2 34.5 1.0 O A:HOH2046 4.3 27.8 1.0 CB A:SER232 4.3 48.6 1.0 OD2 A:ASP189 4.3 34.3 1.0 CB A:LYS136 4.5 39.0 1.0 C A:LYS136 4.6 37.5 1.0 OE1 A:GLU160 4.7 32.8 1.0 CG2 A:THR137 4.7 33.8 1.0 O5' A:ADP1301 4.8 67.7 1.0 O3B A:ADP1301 4.9 67.7 1.0 CG A:ASN234 5.0 66.7 1.0

Magnesium binding site 2 out of 3 in the P4 Protein From Bacteriophage PHI12 K241C Mutant in Complex with Adp and Mgcl


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of P4 Protein From Bacteriophage PHI12 K241C Mutant in Complex with Adp and Mgcl within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1301 b:59.8 occ:1.00 OG1 B:THR137 2.2 34.6 1.0 O2B B:ADP1300 2.4 68.2 1.0 O2A B:ADP1300 3.0 67.9 1.0 CB B:THR137 3.3 34.2 1.0 OG B:SER232 3.3 49.1 1.0 N B:THR137 3.4 35.8 1.0 OD1 B:ASP189 3.6 35.0 1.0 PB B:ADP1300 3.6 68.8 1.0 O B:HOH2060 3.6 43.4 1.0 CA B:THR137 3.7 34.2 1.0 O1B B:ADP1300 3.8 67.8 1.0 CB B:LYS136 4.0 38.9 1.0 PA B:ADP1300 4.1 68.3 1.0 ND2 B:ASN234 4.2 66.8 1.0 O3A B:ADP1300 4.2 68.7 1.0 C B:LYS136 4.2 37.5 1.0 OD2 B:ASP189 4.3 33.5 1.0 CG B:ASP189 4.3 33.6 1.0 CB B:SER232 4.4 48.7 1.0 CG2 B:THR137 4.6 34.0 1.0 O5' B:ADP1300 4.6 67.7 1.0 CA B:LYS136 4.6 38.9 1.0 OE2 B:GLU160 4.6 34.1 1.0 O B:HOH2043 4.8 24.2 1.0 O3B B:ADP1300 4.9 68.2 1.0 N B:LYS136 5.0 40.9 1.0

Magnesium binding site 3 out of 3 in the P4 Protein From Bacteriophage PHI12 K241C Mutant in Complex with Adp and Mgcl


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of P4 Protein From Bacteriophage PHI12 K241C Mutant in Complex with Adp and Mgcl within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg1302 b:59.2 occ:1.00 OG1 C:THR137 2.2 34.8 1.0 O2B C:ADP1301 2.5 67.8 1.0 O2A C:ADP1301 3.2 67.5 1.0 CB C:THR137 3.4 34.0 1.0 OD1 C:ASP189 3.4 35.0 1.0 OG C:SER232 3.4 49.0 1.0 N C:THR137 3.5 35.6 1.0 PB C:ADP1301 3.5 68.0 1.0 O1B C:ADP1301 3.5 67.1 1.0 CA C:THR137 3.8 34.0 1.0 OD2 C:ASP189 4.1 34.7 1.0 CG C:ASP189 4.1 34.2 1.0 O3A C:ADP1301 4.1 67.9 1.0 CB C:LYS136 4.2 38.7 1.0 ND2 C:ASN234 4.2 66.3 1.0 PA C:ADP1301 4.3 67.7 1.0 CB C:SER232 4.3 48.6 1.0 C C:LYS136 4.3 37.3 1.0 CG2 C:THR137 4.6 34.0 1.0 O C:HOH2042 4.7 22.4 1.0 CA C:LYS136 4.8 38.6 1.0 O3B C:ADP1301 4.8 67.9 1.0 O5' C:ADP1301 4.9 67.8 1.0 OG C:SER190 5.0 39.2 1.0

D.E.Kainov, E.J.Mancini, J.Telenius, J.Lisal, J.M.Grimes, D.H.Bamford, D.I.Stuart, R.Tuma. Structural Basis of Mechanochemical Coupling in A Hexameric Molecular Motor. J.Biol.Chem. V. 283 3607 2008.
ISSN: ISSN 0021-9258
PubMed: 18057007
DOI: 10.1074/JBC.M706366200