Magnesium in PDB 4fpp: Bacterial Phosphotransferase

The structure of Bacterial Phosphotransferase, PDB code: 4fpp was solved by A.Fioravanti, B.Clantin, F.Dewitte, Z.Lens, A.Verger, E.Biondi, V.Villeret, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.97 / 2.20
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	103.540, 210.160, 93.930, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / 26.4

The structure of Bacterial Phosphotransferase also contains other interesting chemical elements:

Nickel

(Ni)

1 atom

The binding sites of Magnesium atom in the Bacterial Phosphotransferase (pdb code 4fpp). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Bacterial Phosphotransferase, PDB code: 4fpp:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Bacterial Phosphotransferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Bacterial Phosphotransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg304 b:93.6 occ:1.00 OD2 A:ASP34 2.7 62.2 1.0 NE A:ARG30 3.3 53.5 1.0 NH2 A:ARG30 3.4 49.1 1.0 CG A:ASP34 3.7 57.2 1.0 CZ A:ARG30 3.8 51.4 1.0 CE2 A:PHE83 4.0 54.9 1.0 CD1 A:LEU31 4.0 50.3 1.0 OG1 A:THR79 4.0 48.1 1.0 CB A:ASP34 4.1 52.6 1.0 NE2 A:GLN134 4.5 45.8 1.0 CD2 A:PHE83 4.5 52.9 1.0 CD A:ARG30 4.5 52.1 1.0 OE1 A:GLN134 4.7 48.8 1.0 OD1 A:ASP34 4.8 61.3 1.0 CG2 A:THR79 4.9 45.9 1.0 CZ A:PHE83 4.9 55.9 1.0 CA A:LEU31 4.9 49.6 1.0 CG A:LEU31 5.0 50.3 1.0

Magnesium binding site 2 out of 3 in the Bacterial Phosphotransferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Bacterial Phosphotransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:98.7 occ:1.00 OD2 B:ASP34 3.0 71.3 1.0 NH2 B:ARG30 3.6 68.3 1.0 OE1 B:GLN134 3.6 75.6 1.0 NE2 B:GLN134 3.8 66.5 1.0 CG B:ASP34 3.9 67.5 1.0 CB B:ASP34 4.2 61.9 1.0 CD B:GLN134 4.2 68.9 1.0 OG1 B:THR79 4.2 60.4 1.0 NE B:ARG30 4.3 65.1 1.0 CZ B:ARG30 4.4 67.1 1.0 CE2 B:PHE78 4.7 63.8 1.0 CD2 B:PHE78 4.8 64.5 1.0 CG B:LEU75 5.0 66.0 1.0 CE2 B:PHE83 5.0 65.7 1.0

Magnesium binding site 3 out of 3 in the Bacterial Phosphotransferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Bacterial Phosphotransferase within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg302 b:93.3 occ:1.00 OD2 C:ASP34 3.1 68.7 1.0 NE2 C:GLN134 3.5 47.5 1.0 OE1 C:GLN134 3.6 55.5 1.0 NH2 C:ARG30 3.7 53.5 1.0 CD C:GLN134 4.0 48.9 1.0 CG C:ASP34 4.0 60.4 1.0 OG1 C:THR79 4.0 47.3 1.0 CE2 C:PHE78 4.2 46.4 1.0 CD2 C:PHE78 4.2 45.2 1.0 CE2 C:PHE83 4.3 54.0 1.0 NE C:ARG30 4.4 58.8 1.0 CB C:ASP34 4.5 55.8 1.0 CZ C:ARG30 4.5 55.8 1.0 OD1 C:ASP34 4.9 63.0 1.0 CD2 C:PHE83 4.9 53.8 1.0

A.Fioravanti, B.Clantin, F.Dewitte, Z.Lens, A.Verger, E.G.Biondi, V.Villeret. Structural Insights Into Chpt, An Essential Dimeric Histidine Phosphotransferase Regulating the Cell Cycle in Caulobacter Crescentus. Acta Crystallogr.,Sect.F V. 68 1025 2012.
ISSN: ESSN 1744-3091
PubMed: 22949187
DOI: 10.1107/S1744309112033064