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Magnesium in PDB 5ofb: Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L

Protein crystallography data

The structure of Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L, PDB code: 5ofb was solved by C.H.Douse, Y.Liu, Y.Modis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 79.63 / 2.02
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 69.850, 124.680, 80.360, 90.00, 97.73, 90.00
R / Rfree (%) 19.8 / 22.8

Other elements in 5ofb:

The structure of Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L (pdb code 5ofb). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L, PDB code: 5ofb:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 5ofb

Go back to Magnesium Binding Sites List in 5ofb
Magnesium binding site 1 out of 3 in the Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L


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 Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg703

b:30.3
occ:1.00
O1G B:ATP702 1.9 29.5 1.0
O2B B:ATP702 2.0 30.6 1.0
OD1 B:ASN39 2.1 30.7 1.0
O B:HOH908 2.1 31.9 1.0
O2A B:ATP702 2.2 27.5 1.0
O B:HOH842 2.2 29.2 1.0
PB B:ATP702 3.0 27.4 1.0
CG B:ASN39 3.1 29.7 1.0
PG B:ATP702 3.2 27.7 1.0
PA B:ATP702 3.3 27.9 1.0
O3B B:ATP702 3.4 26.5 1.0
O3A B:ATP702 3.5 30.1 1.0
ND2 B:ASN39 3.6 29.4 1.0
O B:HOH818 3.8 31.7 1.0
O B:HOH870 3.9 30.3 1.0
O5' B:ATP702 4.1 27.2 1.0
OE2 B:GLU35 4.1 35.4 1.0
O2G B:ATP702 4.2 26.9 1.0
CA B:GLY98 4.2 32.2 1.0
O3G B:ATP702 4.2 28.5 1.0
O B:GLU35 4.3 28.6 1.0
O1B B:ATP702 4.4 28.1 1.0
CB B:ASN39 4.5 32.0 1.0
CA B:GLY103 4.5 30.2 1.0
N B:GLY103 4.6 30.2 1.0
O1A B:ATP702 4.6 29.0 1.0
N B:ASN39 4.7 28.9 1.0
CA B:ASN39 4.7 30.9 1.0
N B:LEU104 4.7 30.0 1.0
OD2 B:ASP42 4.8 35.1 1.0
N B:GLY98 5.0 32.5 1.0
C B:GLY103 5.0 29.8 1.0
CB B:ASP38 5.0 31.8 1.0

Magnesium binding site 2 out of 3 in 5ofb

Go back to Magnesium Binding Sites List in 5ofb
Magnesium binding site 2 out of 3 in the Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L


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 Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg704

b:39.7
occ:0.65
O B:ASP69 2.4 35.1 1.0
O B:HOH954 2.4 45.4 1.0
OG B:SER195 2.4 37.9 1.0
O B:GLY70 2.4 34.0 1.0
O B:HOH877 2.6 60.0 1.0
O B:SER195 2.7 35.9 1.0
C B:ASP69 3.1 33.3 1.0
C B:GLY70 3.2 30.1 1.0
C B:SER195 3.3 38.8 1.0
CB B:SER195 3.5 40.3 1.0
N B:GLY70 3.8 32.2 1.0
CA B:SER195 3.8 40.9 1.0
CA B:GLY70 3.9 32.2 1.0
CA B:ASP69 4.0 35.1 1.0
N B:SER195 4.0 45.8 1.0
N B:ALA71 4.1 32.0 1.0
N B:GLY196 4.1 35.0 1.0
O B:HOH962 4.3 63.1 1.0
CB B:ASP69 4.4 35.8 1.0
CA B:ALA71 4.4 34.6 1.0
OD1 B:ASP194 4.5 70.2 1.0
CA B:GLY196 4.5 34.5 1.0
O B:HOH850 4.5 39.4 1.0
OD2 B:ASP194 4.6 62.7 1.0
CG B:ASP194 4.8 61.7 1.0
C B:ALA71 4.9 36.4 1.0

Magnesium binding site 3 out of 3 in 5ofb

Go back to Magnesium Binding Sites List in 5ofb
Magnesium binding site 3 out of 3 in the Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg703

b:36.2
occ:1.00
O A:HOH820 2.0 29.3 1.0
OD1 A:ASN39 2.0 35.6 1.0
O2A A:ATP702 2.1 30.7 1.0
O2G A:ATP702 2.1 33.3 1.0
O2B A:ATP702 2.1 32.1 1.0
O A:HOH870 2.2 34.9 1.0
CG A:ASN39 3.0 35.9 1.0
PA A:ATP702 3.2 32.4 1.0
PB A:ATP702 3.2 31.2 1.0
PG A:ATP702 3.3 32.5 1.0
ND2 A:ASN39 3.3 34.1 1.0
O3A A:ATP702 3.5 31.2 1.0
O3B A:ATP702 3.6 32.7 1.0
O A:HOH835 3.9 37.6 1.0
O A:HOH819 3.9 36.2 1.0
O5' A:ATP702 4.0 33.1 1.0
OE1 A:GLU35 4.0 38.2 1.0
O A:GLU35 4.2 37.4 1.0
O1G A:ATP702 4.3 30.8 1.0
O3G A:ATP702 4.3 32.7 1.0
CB A:ASN39 4.4 36.2 1.0
CA A:GLY103 4.4 33.1 1.0
N A:LEU104 4.5 35.1 1.0
O1A A:ATP702 4.5 31.1 1.0
CA A:GLY98 4.5 38.2 1.0
N A:GLY103 4.5 32.6 1.0
O1B A:ATP702 4.6 35.2 1.0
CA A:ASN39 4.6 36.6 1.0
N A:ASN39 4.7 38.0 1.0
C A:GLY103 4.8 32.3 1.0
OD2 A:ASP42 4.9 46.9 1.0
CB A:ASP38 5.0 34.8 1.0

Reference:

C.H.Douse, S.Bloor, Y.Liu, M.Shamin, I.A.Tchasovnikarova, R.T.Timms, P.J.Lehner, Y.Modis. Neuropathic MORC2 Mutations Perturb Ghkl Atpase Dimerization Dynamics and Epigenetic Silencing By Multiple Structural Mechanisms. Nat Commun V. 9 651 2018.
ISSN: ESSN 2041-1723
PubMed: 29440755
DOI: 10.1038/S41467-018-03045-X
Page generated: Mon Sep 30 00:57:35 2024

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