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Magnesium in PDB 5cmb: Mnemiopsis Leidyi ML032222A Iglur Lbd R703K Mutant Glycine Complex

Protein crystallography data

The structure of Mnemiopsis Leidyi ML032222A Iglur Lbd R703K Mutant Glycine Complex, PDB code: 5cmb 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) 38.99 / 1.34
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 45.731, 123.389, 54.334, 90.00, 112.20, 90.00
R / Rfree (%) 14.3 / 16.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Mnemiopsis Leidyi ML032222A Iglur Lbd R703K Mutant Glycine Complex (pdb code 5cmb). 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 R703K Mutant Glycine Complex, PDB code: 5cmb:

Magnesium binding site 1 out of 1 in 5cmb

Go back to Magnesium Binding Sites List in 5cmb
Magnesium binding site 1 out of 1 in the Mnemiopsis Leidyi ML032222A Iglur Lbd R703K 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 R703K Mutant Glycine Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:8.9
occ:0.69
OE2 A:GLU213 2.0 14.7 1.0
OE2 B:GLU213 2.0 14.5 1.0
OD1 B:ASP110 2.1 14.2 1.0
OD1 A:ASP110 2.1 14.8 1.0
O A:HOH431 2.1 14.1 1.0
O B:HOH421 2.1 13.1 1.0
CD B:GLU213 3.0 13.2 1.0
CD A:GLU213 3.0 11.9 1.0
HH22 B:ARG236 3.1 20.4 1.0
HH22 A:ARG236 3.1 19.6 1.0
CG B:ASP110 3.2 16.3 1.0
CG A:ASP110 3.2 17.8 1.0
OE1 B:GLU213 3.3 14.7 1.0
OE1 A:GLU213 3.3 14.0 1.0
HH12 A:ARG236 3.4 21.6 1.0
HH12 B:ARG236 3.5 18.9 1.0
OD2 A:ASP110 3.7 18.8 1.0
OD2 B:ASP110 3.7 19.1 1.0
NH2 B:ARG236 3.9 17.0 1.0
NH2 A:ARG236 4.0 16.3 1.0
O A:HOH429 4.0 17.0 1.0
O B:HOH436 4.0 18.4 1.0
NH1 A:ARG236 4.2 18.0 1.0
NH1 B:ARG236 4.2 15.7 1.0
HA B:ASP110 4.2 15.1 1.0
HA A:ASP110 4.3 16.6 1.0
H A:ASP110 4.3 15.8 1.0
CG B:GLU213 4.3 11.4 1.0
H B:ASP110 4.3 14.1 1.0
CG A:GLU213 4.3 12.2 1.0
CB B:ASP110 4.3 13.4 1.0
CB A:ASP110 4.4 14.2 1.0
HG2 B:PRO107 4.4 19.8 1.0
HG2 A:GLU213 4.5 14.6 1.0
HG2 B:GLU213 4.5 13.6 1.0
N A:ASP110 4.5 13.2 1.0
N B:ASP110 4.5 11.7 1.0
HH21 B:ARG236 4.5 20.4 1.0
CZ B:ARG236 4.5 14.2 1.0
HG2 A:PRO107 4.5 23.2 1.0
CZ A:ARG236 4.5 16.3 1.0
HH21 A:ARG236 4.6 19.6 1.0
CA B:ASP110 4.6 12.6 1.0
HG3 B:GLU213 4.6 13.6 1.0
CA A:ASP110 4.6 13.8 1.0
HG3 A:GLU213 4.6 14.6 1.0
HB2 B:ASP110 4.6 16.1 1.0
HB2 A:ASP110 4.7 17.1 1.0
HB2 A:PRO107 4.8 20.7 1.0
HB2 B:PRO107 4.8 16.1 1.0
HH11 A:ARG236 4.9 21.6 1.0
HH11 B:ARG236 4.9 18.9 1.0
HG3 B:PRO107 4.9 19.8 1.0
HG3 A:PRO107 5.0 23.2 1.0

Reference:

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
Page generated: Sun Sep 29 02:14:05 2024

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