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:
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
|