Magnesium in PDB 4pfw: Crystal Structure of Mannohexaose Bound Oligopeptide Abc Transporter, Periplasmic Oligopeptide-Binding Protein (TM1226) From Thermotoga Maritima at 2.2 A Resolution

The structure of Crystal Structure of Mannohexaose Bound Oligopeptide Abc Transporter, Periplasmic Oligopeptide-Binding Protein (TM1226) From Thermotoga Maritima at 2.2 A Resolution, PDB code: 4pfw was solved by X.Lu, S.Ghimire-Rijal, M.J.Cuneo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.86 / 2.20
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	99.548, 194.227, 159.425, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 21.8

The binding sites of Magnesium atom in the Crystal Structure of Mannohexaose Bound Oligopeptide Abc Transporter, Periplasmic Oligopeptide-Binding Protein (TM1226) From Thermotoga Maritima at 2.2 A Resolution (pdb code 4pfw). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Mannohexaose Bound Oligopeptide Abc Transporter, Periplasmic Oligopeptide-Binding Protein (TM1226) From Thermotoga Maritima at 2.2 A Resolution, PDB code: 4pfw:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Mannohexaose Bound Oligopeptide Abc Transporter, Periplasmic Oligopeptide-Binding Protein (TM1226) From Thermotoga Maritima at 2.2 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Mannohexaose Bound Oligopeptide Abc Transporter, Periplasmic Oligopeptide-Binding Protein (TM1226) From Thermotoga Maritima at 2.2 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:59.2 occ:1.00 OD1 A:ASN364 2.0 68.5 1.0 OD1 A:ASP362 2.3 61.6 1.0 OD1 A:ASP366 2.3 73.8 1.0 OE1 A:GLU370 2.4 54.9 1.0 O A:PHE368 2.5 56.6 1.0 OE2 A:GLU370 2.6 64.7 1.0 CD A:GLU370 2.9 60.8 1.0 CG A:ASN364 3.1 67.8 1.0 CG A:ASP366 3.1 74.8 1.0 CG A:ASP362 3.4 59.1 1.0 OD2 A:ASP366 3.5 77.2 1.0 C A:PHE368 3.5 52.7 1.0 ND2 A:ASN364 3.7 74.7 1.0 N A:ASP366 3.8 61.9 1.0 N A:PHE368 3.9 48.2 1.0 N A:ASN364 4.1 70.9 1.0 CA A:PHE368 4.1 52.9 1.0 CA A:ASP362 4.1 56.6 1.0 N A:VAL363 4.2 59.8 1.0 CB A:ASP362 4.2 57.1 1.0 OD2 A:ASP362 4.2 61.2 1.0 N A:GLY365 4.2 72.4 1.0 CB A:PHE368 4.2 51.6 1.0 CB A:ASP366 4.2 68.3 1.0 CB A:ASN364 4.3 67.2 1.0 CG A:GLU370 4.4 64.4 1.0 CA A:ASP366 4.4 58.6 1.0 N A:GLY367 4.4 54.3 1.0 CA A:ASN364 4.6 67.3 1.0 C A:ASP362 4.6 58.0 1.0 C A:ASP366 4.6 57.4 1.0 N A:ARG369 4.6 54.8 1.0 C A:ASN364 4.7 71.8 1.0 C A:GLY365 4.9 69.7 1.0 N A:GLU370 4.9 67.1 1.0 C A:GLY367 4.9 53.1 1.0 CA A:ARG369 4.9 63.4 1.0 C A:ARG369 4.9 66.3 1.0 CA A:GLY365 5.0 71.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Mannohexaose Bound Oligopeptide Abc Transporter, Periplasmic Oligopeptide-Binding Protein (TM1226) From Thermotoga Maritima at 2.2 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Mannohexaose Bound Oligopeptide Abc Transporter, Periplasmic Oligopeptide-Binding Protein (TM1226) From Thermotoga Maritima at 2.2 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:68.9 occ:1.00 OD1 B:ASP366 2.1 85.5 1.0 OD1 B:ASN364 2.2 84.6 1.0 O B:PHE368 2.3 65.9 1.0 OD1 B:ASP362 2.3 93.5 1.0 OE1 B:GLU370 2.4 85.4 1.0 OE2 B:GLU370 2.6 88.4 1.0 CD B:GLU370 2.8 87.0 1.0 CG B:ASP366 3.1 82.9 1.0 CG B:ASP362 3.2 89.2 1.0 CG B:ASN364 3.3 86.4 1.0 C B:PHE368 3.4 67.7 1.0 OD2 B:ASP366 3.5 78.8 1.0 N B:PHE368 3.6 71.0 1.0 ND2 B:ASN364 3.8 76.8 1.0 CA B:ASP362 3.9 77.1 1.0 CA B:PHE368 3.9 65.0 1.0 N B:VAL363 4.0 87.6 1.0 CB B:ASP362 4.0 79.3 1.0 N B:ASP366 4.0 82.4 1.0 N B:ASN364 4.0 96.1 1.0 OD2 B:ASP362 4.0 90.5 1.0 CB B:PHE368 4.1 63.7 1.0 CB B:ASP366 4.3 82.8 1.0 C B:ASP362 4.3 88.5 1.0 N B:GLY365 4.3 99.5 1.0 N B:GLY367 4.3 81.7 1.0 CG B:GLU370 4.3 87.4 1.0 CB B:ASN364 4.5 82.2 1.0 CA B:ASP366 4.5 77.0 1.0 N B:ARG369 4.5 64.9 1.0 CA B:ASN364 4.6 99.8 1.0 C B:ASP366 4.7 82.1 1.0 O B:HOH848 4.7 57.7 1.0 C B:ASN364 4.8 0.0 1.0 C B:GLY367 4.8 72.4 1.0 N B:GLU370 4.8 71.1 1.0 C B:ARG369 4.9 68.3 1.0 CA B:ARG369 4.9 65.0 1.0 C B:GLY365 5.0 89.2 1.0 C B:VAL363 5.0 93.8 1.0

S.Ghimire-Rijal, X.Lu, D.A.Myles, M.J.Cuneo. Duplication of Genes in An Atp-Binding Cassette Transport System Increases Dynamic Range While Maintaining Ligand Specificity. J.Biol.Chem. V. 289 30090 2014.
ISSN: ESSN 1083-351X
PubMed: 25210043
DOI: 10.1074/JBC.M114.590992