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Magnesium in PDB 9cdg: MORC2 Atpase Dead Mutant - S87A

Other elements in 9cdg:

The structure of MORC2 Atpase Dead Mutant - S87A also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the MORC2 Atpase Dead Mutant - S87A (pdb code 9cdg). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the MORC2 Atpase Dead Mutant - S87A, PDB code: 9cdg:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 9cdg

Go back to Magnesium Binding Sites List in 9cdg
Magnesium binding site 1 out of 3 in the MORC2 Atpase Dead Mutant - S87A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of MORC2 Atpase Dead Mutant - S87A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1103

b:87.2
occ:1.00
O2A A:ATP1102 2.1 74.3 1.0
O2B A:ATP1102 2.1 86.0 1.0
O2G A:ATP1102 2.1 88.4 1.0
O3B A:ATP1102 2.1 85.1 1.0
PB A:ATP1102 2.4 84.2 1.0
PG A:ATP1102 2.5 82.7 1.0
O3A A:ATP1102 2.7 84.3 1.0
OD1 A:ASN39 2.8 80.4 1.0
PA A:ATP1102 2.8 85.2 1.0
O1G A:ATP1102 3.1 81.0 1.0
OE1 A:GLU35 3.2 95.9 1.0
N A:GLY103 3.5 76.2 1.0
O1A A:ATP1102 3.5 89.4 1.0
CG A:ASN39 3.7 79.4 1.0
CA A:GLY103 3.7 72.5 1.0
O1B A:ATP1102 3.8 83.4 1.0
O3G A:ATP1102 3.9 83.0 1.0
N A:LEU104 3.9 70.9 1.0
ND2 A:ASN39 3.9 80.5 1.0
O5' A:ATP1102 4.2 81.3 1.0
CD A:GLU35 4.2 93.6 1.0
C A:GLY103 4.3 71.7 1.0
N A:ASN102 4.3 75.3 1.0
C A:ASN102 4.6 77.6 1.0
CA A:GLY98 4.6 85.2 1.0
OE2 A:GLU35 4.7 92.7 1.0
N A:GLY101 4.9 80.2 1.0
C A:GLY101 5.0 82.0 1.0
CA A:GLY101 5.0 81.4 1.0

Magnesium binding site 2 out of 3 in 9cdg

Go back to Magnesium Binding Sites List in 9cdg
Magnesium binding site 2 out of 3 in the MORC2 Atpase Dead Mutant - S87A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of MORC2 Atpase Dead Mutant - S87A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1103

b:85.4
occ:1.00
O2A B:ATP1102 2.1 77.0 1.0
O2B B:ATP1102 2.1 88.2 1.0
O1G B:ATP1102 2.1 88.9 1.0
O3B B:ATP1102 2.1 86.5 1.0
PB B:ATP1102 2.4 87.5 1.0
PG B:ATP1102 2.5 84.9 1.0
O3A B:ATP1102 2.8 86.2 1.0
OD1 B:ASN39 2.8 79.9 1.0
PA B:ATP1102 2.9 85.1 1.0
O2G B:ATP1102 3.2 84.6 1.0
N B:GLY103 3.6 76.5 1.0
O1A B:ATP1102 3.6 87.8 1.0
CG B:ASN39 3.7 79.0 1.0
ND2 B:ASN39 3.8 80.6 1.0
CA B:GLY103 3.8 72.9 1.0
O3G B:ATP1102 3.8 82.9 1.0
O1B B:ATP1102 3.8 85.7 1.0
N B:LEU104 4.0 73.5 1.0
O5' B:ATP1102 4.2 84.0 1.0
C B:GLY103 4.2 73.8 1.0
CG B:GLU35 4.5 86.1 1.0
CA B:GLY98 4.5 86.3 1.0
N B:ASN102 4.7 78.0 1.0
C B:ASN102 4.8 79.5 1.0
N B:GLY101 4.9 83.5 1.0
OE2 B:GLU35 4.9 88.1 1.0
CD B:GLU35 4.9 88.3 1.0

Magnesium binding site 3 out of 3 in 9cdg

Go back to Magnesium Binding Sites List in 9cdg
Magnesium binding site 3 out of 3 in the MORC2 Atpase Dead Mutant - S87A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of MORC2 Atpase Dead Mutant - S87A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1104

b:88.8
occ:0.43
O B:SER195 2.1 84.9 1.0
OG B:SER195 2.1 89.5 1.0
O B:GLY70 2.2 89.8 1.0
O B:ASP69 2.5 82.8 1.0
C B:SER195 2.7 82.2 1.0
C B:ASP69 3.1 78.6 1.0
CB B:SER195 3.2 89.7 1.0
C B:GLY70 3.3 83.7 1.0
CA B:SER195 3.3 88.9 1.0
N B:SER195 3.6 91.8 1.0
N B:GLY196 3.6 73.8 1.0
N B:GLY70 3.7 77.2 1.0
CA B:GLY70 3.9 77.2 1.0
CA B:ASP69 4.0 76.3 1.0
CA B:GLY196 4.1 73.8 1.0
N B:ALA71 4.3 82.3 1.0
CB B:ASP69 4.4 81.7 1.0
CA B:ALA71 4.6 82.3 1.0
C B:ALA71 4.9 81.4 1.0
OD1 B:ASP194 4.9 103.0 1.0
C B:ASP194 4.9 90.0 1.0

Reference:

W.Tan, J.Park, H.Venugopal, J.Lou, P.S.Dias, P.L.Baldoni, K.W.Moon, T.A.Dite, C.R.Keenan, A.D.Gurzau, J.Lee, T.M.Johanson, A.Leis, J.Yousef, V.Vaibhav, L.F.Dagley, C.S.Ang, L.D.Corso, C.Davidovich, S.J.Vervoort, G.K.Smyth, M.E.Blewitt, R.S.Allan, E.Hinde, S.D'arcy, J.K.Ryu, S.Shakeel. MORC2 Is A Phosphorylation-Dependent Dna Compaction Machine. Nat Commun V. 16 5606 2025.
ISSN: ESSN 2041-1723
PubMed: 40593625
DOI: 10.1038/S41467-025-60751-Z
Page generated: Sat Aug 16 00:07:11 2025

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