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Magnesium in PDB 4fpp: Bacterial Phosphotransferase

Protein crystallography data

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

Other elements in 4fpp:

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

Nickel (Ni) 1 atom

Magnesium Binding Sites:

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 4fpp

Go back to Magnesium Binding Sites List in 4fpp
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 4fpp

Go back to Magnesium Binding Sites List in 4fpp
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 4fpp

Go back to Magnesium Binding Sites List in 4fpp
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

Reference:

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
Page generated: Mon Dec 14 15:37:02 2020

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