Magnesium in PDB 4ak8: Structure of F241L Mutant of Langerin Carbohydrate Recognition Domain.

The structure of Structure of F241L Mutant of Langerin Carbohydrate Recognition Domain., PDB code: 4ak8 was solved by E.Chabrol, M.Thepaut, C.Dezutter-Dambuyant, C.Vives, J.Marcoux, R.Kahn, J.Valadeau-Guilemond, P.Vachette, D.Durand, F.Fieschi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.52 / 1.40
Space group	P 42
Cell size a, b, c (Å), α, β, γ (°)	79.959, 79.959, 90.419, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 21.9

The structure of Structure of F241L Mutant of Langerin Carbohydrate Recognition Domain. also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Calcium	(Ca)	4 atoms

The binding sites of Magnesium atom in the Structure of F241L Mutant of Langerin Carbohydrate Recognition Domain. (pdb code 4ak8). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Structure of F241L Mutant of Langerin Carbohydrate Recognition Domain., PDB code: 4ak8:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Structure of F241L Mutant of Langerin Carbohydrate Recognition Domain.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of F241L Mutant of Langerin Carbohydrate Recognition Domain. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1327 b:20.2 occ:1.00 OH A:TYR208 2.9 30.5 1.0 N A:LEU211 3.2 13.2 1.0 N A:ILE212 3.7 17.0 1.0 CB A:SER210 3.7 11.8 1.0 CE2 A:TYR208 3.8 19.0 1.0 CZ A:TYR208 3.8 21.9 1.0 CA A:SER210 3.9 10.9 1.0 CA A:LEU211 4.0 15.2 1.0 C A:SER210 4.1 11.9 1.0 CB A:ILE212 4.1 21.1 1.0 CB A:LEU211 4.2 19.1 1.0 C A:LEU211 4.3 17.3 1.0 CG1 A:ILE212 4.4 24.6 1.0 CZ A:PHE222 4.4 27.4 1.0 CA A:ILE212 4.5 18.5 1.0 OG A:SER210 4.7 11.6 1.0 O A:ILE212 4.7 15.8 1.0 CE2 A:PHE222 4.8 30.3 1.0 CZ A:PHE317 4.9 13.5 1.0 CG A:LEU211 4.9 16.9 1.0 CE1 A:PHE222 5.0 21.6 1.0

Magnesium binding site 2 out of 4 in the Structure of F241L Mutant of Langerin Carbohydrate Recognition Domain.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of F241L Mutant of Langerin Carbohydrate Recognition Domain. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1327 b:20.3 occ:1.00 OH B:TYR208 2.8 22.9 1.0 N B:LEU211 3.2 15.5 1.0 N B:ILE212 3.6 19.5 1.0 CB B:SER210 3.7 13.2 1.0 CE2 B:TYR208 3.8 18.2 1.0 CD1 B:ILE212 3.8 34.1 1.0 CZ B:TYR208 3.8 19.7 1.0 CA B:SER210 3.9 11.3 1.0 CB B:ILE212 4.0 23.0 1.0 CG1 B:ILE212 4.0 31.1 1.0 CA B:LEU211 4.0 18.8 1.0 C B:SER210 4.1 12.9 1.0 CB B:LEU211 4.2 17.9 1.0 C B:LEU211 4.3 17.6 1.0 CA B:ILE212 4.4 21.8 1.0 CZ B:PHE222 4.6 26.9 1.0 OG B:SER210 4.7 12.2 1.0 O B:ILE212 4.7 19.1 1.0 CZ B:PHE317 4.8 10.0 1.0 CG B:LEU211 4.8 22.3 1.0

Magnesium binding site 3 out of 4 in the Structure of F241L Mutant of Langerin Carbohydrate Recognition Domain.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of F241L Mutant of Langerin Carbohydrate Recognition Domain. within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg1327 b:21.7 occ:1.00 OH C:TYR208 2.9 21.4 1.0 N C:LEU211 3.0 15.9 1.0 CA C:SER210 3.7 14.3 1.0 CG1 C:ILE212 3.7 26.9 1.0 N C:ILE212 3.8 19.9 1.0 CZ C:TYR208 3.8 15.8 1.0 CE2 C:TYR208 3.8 14.7 1.0 CB C:SER210 3.9 13.3 1.0 CA C:LEU211 3.9 18.9 1.0 C C:SER210 3.9 14.8 1.0 CB C:LEU211 4.1 20.8 1.0 CD1 C:ILE212 4.1 35.4 1.0 C C:LEU211 4.2 19.9 1.0 CG2 C:ILE212 4.4 24.2 1.0 CB C:ILE212 4.5 22.1 1.0 CG C:LEU211 4.6 21.6 1.0 CA C:ILE212 4.8 22.0 1.0 CZ C:PHE222 4.8 28.7 1.0 OG C:SER210 4.9 14.8 1.0

Magnesium binding site 4 out of 4 in the Structure of F241L Mutant of Langerin Carbohydrate Recognition Domain.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of F241L Mutant of Langerin Carbohydrate Recognition Domain. within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg1331 b:13.8 occ:1.00 OH D:TYR208 3.0 15.5 1.0 O D:HOH2199 3.1 18.1 1.0 N D:LEU211 3.1 11.2 1.0 CG1 D:ILE212 3.5 23.6 1.0 N D:ILE212 3.6 12.5 1.0 CB D:SER210 3.7 10.6 1.0 CE2 D:TYR208 3.8 11.2 1.0 CA D:SER210 3.8 8.6 1.0 CZ D:TYR208 3.9 13.5 1.0 C D:SER210 4.0 10.2 1.0 CA D:LEU211 4.0 13.3 1.0 CB D:LEU211 4.2 11.8 1.0 CD1 D:ILE212 4.2 32.9 1.0 C D:LEU211 4.3 14.7 1.0 CZ D:PHE222 4.3 19.3 1.0 CB D:ILE212 4.5 18.9 1.0 CA D:ILE212 4.6 14.4 1.0 CG2 D:ILE212 4.6 21.7 1.0 CE2 D:PHE222 4.6 25.6 1.0 OG D:SER210 4.6 11.1 1.0 CG D:LEU211 4.7 14.8 1.0 CZ D:PHE317 4.8 10.3 1.0 O D:ILE212 4.8 15.6 1.0 CE1 D:PHE222 4.9 16.3 1.0 O D:HOH2003 4.9 17.3 1.0

E.Chabrol, M.Thepaut, C.Dezutter-Dambuyant, C.Vives, J.Marcoux, R.Kahn, J.Valladeau-Guilemond, P.Vachette, D.Durand, F.Fieschi. Alteration of the Langerin Oligomerization State Affects Birbeck Granule Formation. Biophys.J. V. 108 666 2015.
ISSN: ISSN 0006-3495
PubMed: 25650933
DOI: 10.1016/J.BPJ.2014.10.075