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Magnesium in PDB 6nm9: Cryoem Structure of the LBCAS12A-Crrna-ACRVA4 Dimer

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryoem Structure of the LBCAS12A-Crrna-ACRVA4 Dimer (pdb code 6nm9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Cryoem Structure of the LBCAS12A-Crrna-ACRVA4 Dimer, PDB code: 6nm9:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 6nm9

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Magnesium binding site 1 out of 4 in the Cryoem Structure of the LBCAS12A-Crrna-ACRVA4 Dimer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryoem Structure of the LBCAS12A-Crrna-ACRVA4 Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:79.7
occ:1.00
NZ A:LYS202 2.0 0.7 1.0
OP2 G:A10 3.4 96.4 1.0
CE A:LYS202 3.4 0.7 1.0
OP2 G:A3 4.1 0.1 1.0
O4 G:U5 4.1 0.1 1.0
OP2 G:U9 4.2 96.2 1.0
CD A:LYS202 4.5 0.7 1.0
N7 G:A10 4.7 96.4 1.0
O5' G:U9 4.7 96.2 1.0
P G:A10 4.8 96.4 1.0
C5 G:C11 4.8 99.5 1.0
OP2 G:A4 4.8 0.1 1.0
C8 G:A10 5.0 96.4 1.0

Magnesium binding site 2 out of 4 in 6nm9

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Magnesium binding site 2 out of 4 in the Cryoem Structure of the LBCAS12A-Crrna-ACRVA4 Dimer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryoem Structure of the LBCAS12A-Crrna-ACRVA4 Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1301

b:98.5
occ:1.00
OP2 G:A19 1.9 99.0 1.0
O B:THR716 2.4 0.9 1.0
P G:A19 3.3 99.0 1.0
OD1 B:ASN718 3.3 0.2 1.0
C B:THR716 3.6 0.9 1.0
O5' G:A19 3.8 99.0 1.0
NZ B:LYS707 4.1 0.3 1.0
OP1 G:A19 4.2 99.0 1.0
C B:PRO717 4.3 0.6 1.0
O3' G:U18 4.3 0.6 1.0
CA B:PRO717 4.3 0.6 1.0
C3' G:U18 4.4 0.6 1.0
N B:PRO717 4.4 0.6 1.0
O B:PRO717 4.5 0.6 1.0
CG B:ASN718 4.5 0.2 1.0
O5' G:U18 4.5 0.6 1.0
N B:ASN718 4.6 0.2 1.0
N B:THR716 4.6 0.9 1.0
CA B:THR716 4.6 0.9 1.0
OP2 G:U18 4.8 0.6 1.0
N7 G:A19 4.8 99.0 1.0
C8 G:A19 4.8 99.0 1.0
OP1 G:U18 4.9 0.6 1.0
OD1 B:ASP708 4.9 0.1 1.0
OP2 G:G20 5.0 100.0 1.0
P G:U18 5.0 0.6 1.0
CB B:THR716 5.0 0.9 1.0

Magnesium binding site 3 out of 4 in 6nm9

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Magnesium binding site 3 out of 4 in the Cryoem Structure of the LBCAS12A-Crrna-ACRVA4 Dimer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Cryoem Structure of the LBCAS12A-Crrna-ACRVA4 Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg301

b:78.6
occ:1.00
NZ C:LYS202 2.1 0.7 1.0
OP2 E:A10 3.4 96.6 1.0
CE C:LYS202 3.5 0.7 1.0
OP2 E:A3 4.1 0.5 1.0
O4 E:U5 4.1 0.4 1.0
OP2 E:U9 4.2 96.2 1.0
CD C:LYS202 4.7 0.7 1.0
N7 E:A10 4.7 96.6 1.0
O5' E:U9 4.7 96.2 1.0
P E:A10 4.8 96.6 1.0
C5 E:C11 4.8 99.8 1.0
OP2 E:A4 4.8 0.8 1.0
C8 E:A10 5.0 96.6 1.0

Magnesium binding site 4 out of 4 in 6nm9

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Magnesium binding site 4 out of 4 in the Cryoem Structure of the LBCAS12A-Crrna-ACRVA4 Dimer


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Cryoem Structure of the LBCAS12A-Crrna-ACRVA4 Dimer within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1301

b:95.4
occ:1.00
OP2 E:A19 2.1 98.7 1.0
O D:THR716 2.4 99.1 1.0
OD1 D:ASN718 3.3 0.3 1.0
P E:A19 3.5 98.7 1.0
C D:THR716 3.6 99.1 1.0
O5' E:A19 4.0 98.7 1.0
NZ D:LYS707 4.1 0.6 1.0
C D:PRO717 4.3 0.3 1.0
CA D:PRO717 4.3 0.3 1.0
OP1 E:A19 4.4 98.7 1.0
N D:PRO717 4.4 0.3 1.0
O3' E:U18 4.5 0.8 1.0
O D:PRO717 4.5 0.3 1.0
CG D:ASN718 4.5 0.3 1.0
C3' E:U18 4.6 0.8 1.0
N D:THR716 4.6 99.1 1.0
N D:ASN718 4.6 0.3 1.0
CA D:THR716 4.6 99.1 1.0
O5' E:U18 4.6 0.8 1.0
OP2 E:U18 4.8 0.8 1.0
N7 E:A19 4.8 98.7 1.0
C8 E:A19 4.9 98.7 1.0
OD1 D:ASP708 4.9 0.6 1.0
C D:GLY715 5.0 0.1 1.0
OP1 E:U18 5.0 0.8 1.0

Reference:

H.Zhang, Z.Li, C.M.Daczkowski, C.Gabel, A.D.Mesecar, L.Chang. Structural Basis For the Inhibition of Crispr-CAS12A By Anti-Crispr Proteins. Cell Host Microbe V. 25 815 2019.
ISSN: ESSN 1934-6069
PubMed: 31155345
DOI: 10.1016/J.CHOM.2019.05.004
Page generated: Tue Oct 1 12:46:15 2024

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