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Chlorine in PDB 5i58: Glutamate- and Glycine-Bound GLUN1/GLUN2A Agonist Binding Domains with Mpx-004

Protein crystallography data

The structure of Glutamate- and Glycine-Bound GLUN1/GLUN2A Agonist Binding Domains with Mpx-004, PDB code: 5i58 was solved by T.-C.Mou, S.R.Sprang, K.B.Hansen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.13 / 2.52
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.919, 86.425, 122.628, 90.00, 90.00, 90.00
R / Rfree (%) 23.3 / 29.2

Other elements in 5i58:

The structure of Glutamate- and Glycine-Bound GLUN1/GLUN2A Agonist Binding Domains with Mpx-004 also contains other interesting chemical elements:

Fluorine (F) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Glutamate- and Glycine-Bound GLUN1/GLUN2A Agonist Binding Domains with Mpx-004 (pdb code 5i58). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Glutamate- and Glycine-Bound GLUN1/GLUN2A Agonist Binding Domains with Mpx-004, PDB code: 5i58:

Chlorine binding site 1 out of 1 in 5i58

Go back to Chlorine Binding Sites List in 5i58
Chlorine binding site 1 out of 1 in the Glutamate- and Glycine-Bound GLUN1/GLUN2A Agonist Binding Domains with Mpx-004


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Glutamate- and Glycine-Bound GLUN1/GLUN2A Agonist Binding Domains with Mpx-004 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl302

b:39.4
occ:1.00
CL B:67R302 0.0 39.4 1.0
C02 B:67R302 1.7 39.4 1.0
C01 B:67R302 2.6 47.0 1.0
C03 B:67R302 2.7 31.5 1.0
F29 B:67R302 2.8 38.9 1.0
N B:GLU133 2.8 40.3 1.0
C B:VAL132 3.3 26.1 1.0
CA B:GLU133 3.4 31.2 1.0
O B:PRO130 3.4 19.4 1.0
N B:VAL132 3.4 22.7 1.0
CB B:GLU133 3.6 27.8 1.0
C B:PHE131 3.6 27.4 1.0
CA B:VAL132 3.7 25.1 1.0
C06 B:67R302 3.8 35.2 1.0
C B:PRO130 3.9 16.5 1.0
N19 B:67R302 3.9 46.9 1.0
C04 B:67R302 3.9 36.4 1.0
C15 B:67R302 3.9 41.6 1.0
O B:VAL132 4.0 17.6 1.0
O B:PHE131 4.1 38.4 1.0
CA B:PHE131 4.1 18.2 1.0
N B:PHE131 4.2 25.3 1.0
C10 B:67R302 4.2 34.7 1.0
N24 B:67R302 4.2 38.5 1.0
C09 B:67R302 4.3 37.0 1.0
CE2 A:TYR143 4.3 23.1 1.0
C05 B:67R302 4.3 31.4 1.0
CB B:PRO130 4.4 17.2 1.0
C12 B:67R302 4.5 38.0 1.0
CD2 A:TYR143 4.6 22.8 1.0
CG B:GLU133 4.7 27.7 1.0
CA B:PRO130 4.7 23.1 1.0
N22 B:67R302 4.8 33.0 1.0
C B:GLU133 4.9 23.9 1.0
O21 B:67R302 4.9 47.7 1.0
C11 B:67R302 4.9 40.0 1.0
C08 B:67R302 5.0 34.7 1.0

Reference:

F.Yi, T.C.Mou, K.N.Dorsett, R.A.Volkmann, F.S.Menniti, S.R.Sprang, K.B.Hansen. Structural Basis For Negative Allosteric Modulation of GLUN2A-Containing Nmda Receptors. Neuron V. 91 1316 2016.
ISSN: ISSN 0896-6273
PubMed: 27618671
DOI: 10.1016/J.NEURON.2016.08.014
Page generated: Sat Dec 12 11:49:58 2020

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