Magnesium in PDB 5cmc: Mnemiopsis Leidyi ML032222A Iglur Lbd E423S Mutant Glycine Complex

The structure of Mnemiopsis Leidyi ML032222A Iglur Lbd E423S Mutant Glycine Complex, PDB code: 5cmc was solved by M.L.Mayer, A.Thomas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.11 / 1.28
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.899, 123.138, 54.507, 90.00, 111.72, 90.00
R / Rfree (%)	13.4 / 15.7

The binding sites of Magnesium atom in the Mnemiopsis Leidyi ML032222A Iglur Lbd E423S Mutant Glycine Complex (pdb code 5cmc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Mnemiopsis Leidyi ML032222A Iglur Lbd E423S Mutant Glycine Complex, PDB code: 5cmc:

Magnesium binding site 1 out of 1 in the Mnemiopsis Leidyi ML032222A Iglur Lbd E423S Mutant Glycine Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mnemiopsis Leidyi ML032222A Iglur Lbd E423S Mutant Glycine Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:17.4 occ:0.50 OD1 B:ASP110 1.2 28.6 1.0 OE2 A:GLU213 1.8 23.3 1.0 OE2 B:GLU213 1.9 20.4 1.0 OD1 A:ASP110 2.0 23.9 1.0 CG B:ASP110 2.1 26.4 1.0 CD B:GLU213 2.1 22.2 1.0 CD A:GLU213 2.1 25.6 1.0 OE1 B:GLU213 2.2 24.2 1.0 O B:HOH401 2.2 20.5 0.6 OE1 A:GLU213 2.3 27.9 1.0 OD2 B:ASP110 2.7 34.5 1.0 CG A:ASP110 3.0 22.5 1.0 HH22 B:ARG236 3.1 37.9 1.0 HH22 A:ARG236 3.1 31.7 0.8 OD2 A:ASP110 3.4 23.6 1.0 CB B:ASP110 3.6 23.3 1.0 HH12 B:ARG236 3.7 34.3 1.0 CG B:GLU213 3.7 23.9 1.0 CG A:GLU213 3.7 25.8 1.0 HH12 A:ARG236 3.8 26.6 0.8 HA B:ASP110 3.8 19.4 1.0 HB3 B:ASP110 3.9 28.0 1.0 NH2 B:ARG236 3.9 31.5 1.0 NH2 A:ARG236 4.0 26.4 0.8 HG3 A:GLU213 4.0 30.9 1.0 HG2 B:GLU213 4.0 28.7 1.0 HG2 A:GLU213 4.1 30.9 1.0 HG3 B:GLU213 4.1 28.7 1.0 HA A:ASP110 4.2 21.2 1.0 CA B:ASP110 4.2 16.1 1.0 CB A:ASP110 4.3 19.0 1.0 HB2 B:ASP110 4.3 28.0 1.0 O B:HOH505 4.3 32.2 1.0 NH1 B:ARG236 4.4 28.6 1.0 HH21 B:ARG236 4.4 37.9 1.0 HB3 A:ASP110 4.4 22.8 1.0 NH1 A:ARG236 4.5 22.2 0.8 HH21 A:ARG236 4.5 31.7 0.8 HB3 B:GLU213 4.6 19.9 1.0 HB2 B:PRO107 4.6 18.8 1.0 CZ B:ARG236 4.6 29.3 1.0 HG3 B:PRO107 4.6 21.3 1.0 N B:ASP110 4.7 16.1 1.0 CZ A:ARG236 4.7 23.2 0.8 CA A:ASP110 4.7 17.7 1.0 CB B:GLU213 4.7 16.6 1.0 HB3 A:GLU213 4.7 25.4 1.0 HA B:GLU213 4.8 14.8 1.0 O B:HOH511 4.8 35.0 1.0 HG2 B:PRO107 4.8 21.3 1.0 O B:PHE212 4.9 14.0 1.0 H B:ASP110 4.9 19.3 1.0 CB A:GLU213 4.9 21.2 1.0 HG3 A:PRO107 5.0 22.4 1.0 HB2 A:PRO107 5.0 20.5 1.0

A.Yu, R.Alberstein, A.Thomas, A.Zimmet, R.Grey, M.L.Mayer, A.Y.Lau. Molecular Lock Regulates Binding of Glycine to A Primitive Nmda Receptor. Proc.Natl.Acad.Sci.Usa V. 113 E6786 2016.
ISSN: ESSN 1091-6490
PubMed: 27791085
DOI: 10.1073/PNAS.1607010113