Manganese in PDB 2vhc: P4 Protein From Bacteriophage PHI12 N234G Mutant in Complex with Ampcpp and Mn

The structure of P4 Protein From Bacteriophage PHI12 N234G Mutant in Complex with Ampcpp and Mn, PDB code: 2vhc 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)	100.50 / 2.35
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	105.120, 129.518, 158.522, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 23.7

The binding sites of Manganese atom in the P4 Protein From Bacteriophage PHI12 N234G Mutant in Complex with Ampcpp and Mn (pdb code 2vhc). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the P4 Protein From Bacteriophage PHI12 N234G Mutant in Complex with Ampcpp and Mn, PDB code: 2vhc:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the P4 Protein From Bacteriophage PHI12 N234G Mutant in Complex with Ampcpp and Mn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of P4 Protein From Bacteriophage PHI12 N234G Mutant in Complex with Ampcpp and Mn within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1301 b:56.6 occ:1.00 O1B A:APC1300 2.2 56.6 1.0 O2A A:APC1300 2.2 58.2 1.0 O A:HOH2242 2.2 44.1 1.0 O1G A:APC1300 2.3 61.1 1.0 OG1 A:THR137 2.5 36.6 1.0 O A:HOH2243 2.6 56.9 1.0 PB A:APC1300 3.2 59.2 1.0 PG A:APC1300 3.3 62.4 1.0 PA A:APC1300 3.3 60.7 1.0 O A:HOH2172 3.4 49.4 1.0 O3B A:APC1300 3.5 61.4 1.0 CB A:THR137 3.6 38.2 1.0 C3A A:APC1300 3.7 59.3 1.0 O3G A:APC1300 3.8 60.8 1.0 OD1 A:ASP189 4.0 40.1 1.0 N A:THR137 4.0 39.0 1.0 O5' A:APC1300 4.1 60.3 1.0 O A:HOH2187 4.1 36.7 1.0 O A:HOH2241 4.1 38.3 1.0 CA A:THR137 4.3 38.6 1.0 OD2 A:ASP189 4.4 36.2 1.0 O2G A:APC1300 4.6 63.1 1.0 O1A A:APC1300 4.6 61.5 1.0 O2B A:APC1300 4.6 57.7 1.0 CG A:ASP189 4.7 36.5 1.0 OG A:SER232 4.7 46.6 1.0 CG2 A:THR137 4.8 38.9 1.0 CB A:LYS136 4.8 42.5 1.0 OE2 A:GLU160 4.9 46.2 1.0 C A:LYS136 4.9 40.6 1.0

Manganese binding site 2 out of 3 in the P4 Protein From Bacteriophage PHI12 N234G Mutant in Complex with Ampcpp and Mn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of P4 Protein From Bacteriophage PHI12 N234G Mutant in Complex with Ampcpp and Mn within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1301 b:60.0 occ:1.00 O2A B:APC1300 2.2 59.2 1.0 O2B B:APC1300 2.2 55.5 1.0 O B:HOH2247 2.4 35.9 1.0 O1G B:APC1300 2.4 65.1 1.0 OG1 B:THR137 2.4 36.2 1.0 PB B:APC1300 3.1 58.5 1.0 PA B:APC1300 3.3 59.7 1.0 PG B:APC1300 3.4 65.6 1.0 O3B B:APC1300 3.4 62.7 1.0 CB B:THR137 3.5 37.0 1.0 C3A B:APC1300 3.6 60.2 1.0 O B:HOH2172 3.8 56.0 1.0 O B:HOH2242 4.0 38.7 1.0 O5' B:APC1300 4.0 60.2 1.0 O3G B:APC1300 4.0 67.0 1.0 O B:HOH2174 4.1 32.9 1.0 OD1 B:ASP189 4.1 38.6 1.0 N B:THR137 4.1 37.8 1.0 CA B:THR137 4.3 37.1 1.0 OD2 B:ASP189 4.4 39.4 1.0 O1B B:APC1300 4.6 59.7 1.0 O1A B:APC1300 4.6 62.1 1.0 O2G B:APC1300 4.6 68.0 1.0 CG2 B:THR137 4.7 37.4 1.0 CG B:ASP189 4.7 36.8 1.0 NH2 A:ARG272 4.7 47.9 1.0 OG B:SER232 4.8 43.1 1.0 CB B:LYS136 4.9 41.5 1.0

Manganese binding site 3 out of 3 in the P4 Protein From Bacteriophage PHI12 N234G Mutant in Complex with Ampcpp and Mn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of P4 Protein From Bacteriophage PHI12 N234G Mutant in Complex with Ampcpp and Mn within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn1301 b:52.4 occ:1.00 O2A C:APC1300 2.1 57.1 1.0 O C:HOH2234 2.2 44.8 1.0 O2B C:APC1300 2.2 52.8 1.0 O1G C:APC1300 2.4 58.9 1.0 O C:HOH2235 2.4 59.5 1.0 OG1 C:THR137 2.5 33.6 1.0 PB C:APC1300 3.2 54.3 1.0 PG C:APC1300 3.3 58.6 1.0 PA C:APC1300 3.3 57.3 1.0 O3B C:APC1300 3.5 56.9 1.0 CB C:THR137 3.6 34.9 1.0 O3G C:APC1300 3.6 58.3 1.0 C3A C:APC1300 3.7 56.9 1.0 O C:HOH2232 3.7 58.1 1.0 O C:HOH2229 3.8 40.0 1.0 N C:THR137 4.1 36.1 1.0 OD1 C:ASP189 4.2 38.1 1.0 O C:HOH2151 4.3 30.9 1.0 O1A C:APC1300 4.3 60.4 1.0 CA C:THR137 4.4 35.7 1.0 OD2 C:ASP189 4.4 34.1 1.0 O5' C:APC1300 4.5 57.9 1.0 NH2 B:ARG272 4.6 43.2 1.0 O1B C:APC1300 4.6 57.8 1.0 O2G C:APC1300 4.6 59.5 1.0 OG C:SER232 4.7 46.7 1.0 CG C:ASP189 4.7 36.0 1.0 CG2 C:THR137 4.8 34.5 1.0 OE2 C:GLU160 4.8 41.8 1.0 CB C:LYS136 4.9 40.6 1.0 CD C:GLU160 5.0 37.7 1.0 O C:HOH2179 5.0 54.9 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