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Magnesium in PDB 7rlj: Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs.

Enzymatic activity of Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs.

All present enzymatic activity of Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs.:
3.6.4.6;

Magnesium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Magnesium atom in the Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs. (pdb code 7rlj). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 12 binding sites of Magnesium where determined in the Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs., PDB code: 7rlj:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 12 in 7rlj

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Magnesium binding site 1 out of 12 in the Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg802

b:129.1
occ:1.00
 O3G A:AGS801 2.1 152.5 1.0
O2A A:AGS801 2.2 152.5 1.0
OG1 A:THR252 2.3 119.4 1.0
O1B A:AGS801 2.9 152.5 1.0
CB A:THR252 3.0 119.4 1.0
PA A:AGS801 3.3 152.5 1.0
PG A:AGS801 3.5 152.5 1.0
O1A A:AGS801 3.5 152.5 1.0
OD1 A:ASP304 3.5 123.0 1.0
CG2 A:THR252 3.8 119.4 1.0
OD2 A:ASP304 3.8 123.0 1.0
PB A:AGS801 3.9 152.5 1.0
O2G A:AGS801 3.9 152.5 1.0
CG A:ASP304 4.1 123.0 1.0
O3A A:AGS801 4.1 152.5 1.0
O3B A:AGS801 4.2 152.5 1.0
CA A:THR252 4.3 119.4 1.0
N A:THR252 4.4 119.4 1.0
O5' A:AGS801 4.6 152.5 1.0
S1G A:AGS801 4.9 152.5 1.0

Magnesium binding site 2 out of 12 in 7rlj

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Magnesium binding site 2 out of 12 in the Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg802

b:115.7
occ:1.00
 O3G B:AGS801 2.1 147.9 1.0
O2A B:AGS801 2.2 147.9 1.0
OG1 B:THR252 2.3 107.6 1.0
O1B B:AGS801 2.9 147.9 1.0
CB B:THR252 3.0 107.6 1.0
PA B:AGS801 3.3 147.9 1.0
PG B:AGS801 3.5 147.9 1.0
O1A B:AGS801 3.5 147.9 1.0
OD1 B:ASP304 3.5 125.8 1.0
CG2 B:THR252 3.8 107.6 1.0
OD2 B:ASP304 3.8 125.8 1.0
PB B:AGS801 3.9 147.9 1.0
O2G B:AGS801 3.9 147.9 1.0
CG B:ASP304 4.1 125.8 1.0
O3A B:AGS801 4.1 147.9 1.0
O3B B:AGS801 4.2 147.9 1.0
CA B:THR252 4.3 107.6 1.0
N B:THR252 4.4 107.6 1.0
O5' B:AGS801 4.6 147.9 1.0
S1G B:AGS801 4.9 147.9 1.0

Magnesium binding site 3 out of 12 in 7rlj

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Magnesium binding site 3 out of 12 in the Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg802

b:122.1
occ:1.00
 O3G C:AGS801 2.1 89.2 1.0
O2A C:AGS801 2.2 89.2 1.0
OG1 C:THR252 2.3 112.8 1.0
O1B C:AGS801 2.9 89.2 1.0
CB C:THR252 3.0 112.8 1.0
PA C:AGS801 3.3 89.2 1.0
PG C:AGS801 3.5 89.2 1.0
O1A C:AGS801 3.5 89.2 1.0
OD1 C:ASP304 3.5 117.7 1.0
CG2 C:THR252 3.8 112.8 1.0
OD2 C:ASP304 3.8 117.7 1.0
PB C:AGS801 3.9 89.2 1.0
O2G C:AGS801 3.9 89.2 1.0
CG C:ASP304 4.1 117.7 1.0
O3A C:AGS801 4.1 89.2 1.0
O3B C:AGS801 4.2 89.2 1.0
CA C:THR252 4.3 112.8 1.0
N C:THR252 4.4 112.8 1.0
O5' C:AGS801 4.6 89.2 1.0
S1G C:AGS801 4.9 89.2 1.0

Magnesium binding site 4 out of 12 in 7rlj

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Magnesium binding site 4 out of 12 in the Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg802

b:135.4
occ:1.00
 O3G D:AGS801 2.1 152.5 1.0
O2A D:AGS801 2.2 152.5 1.0
OG1 D:THR252 2.3 116.0 1.0
O1B D:AGS801 2.9 152.5 1.0
CB D:THR252 3.0 116.0 1.0
PA D:AGS801 3.3 152.5 1.0
PG D:AGS801 3.5 152.5 1.0
O1A D:AGS801 3.5 152.5 1.0
OD1 D:ASP304 3.5 120.7 1.0
CG2 D:THR252 3.8 116.0 1.0
OD2 D:ASP304 3.8 120.7 1.0
PB D:AGS801 3.9 152.5 1.0
O2G D:AGS801 3.9 152.5 1.0
CG D:ASP304 4.1 120.7 1.0
O3A D:AGS801 4.1 152.5 1.0
O3B D:AGS801 4.2 152.5 1.0
CA D:THR252 4.3 116.0 1.0
N D:THR252 4.4 116.0 1.0
O5' D:AGS801 4.6 152.5 1.0
S1G D:AGS801 4.9 152.5 1.0

Magnesium binding site 5 out of 12 in 7rlj

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Magnesium binding site 5 out of 12 in the Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg802

b:123.0
occ:1.00
 O3G E:AGS801 2.1 140.8 1.0
O2A E:AGS801 2.2 140.8 1.0
OG1 E:THR252 2.3 111.2 1.0
O1B E:AGS801 2.9 140.8 1.0
CB E:THR252 3.0 111.2 1.0
PA E:AGS801 3.3 140.8 1.0
PG E:AGS801 3.5 140.8 1.0
O1A E:AGS801 3.5 140.8 1.0
OD1 E:ASP304 3.5 128.9 1.0
CG2 E:THR252 3.8 111.2 1.0
OD2 E:ASP304 3.8 128.9 1.0
PB E:AGS801 3.9 140.8 1.0
O2G E:AGS801 3.9 140.8 1.0
CG E:ASP304 4.1 128.9 1.0
O3A E:AGS801 4.1 140.8 1.0
O3B E:AGS801 4.2 140.8 1.0
CA E:THR252 4.3 111.2 1.0
N E:THR252 4.4 111.2 1.0
O5' E:AGS801 4.6 140.8 1.0
S1G E:AGS801 4.9 140.8 1.0

Magnesium binding site 6 out of 12 in 7rlj

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Magnesium binding site 6 out of 12 in the Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg802

b:117.6
occ:1.00
 O3G F:AGS801 2.1 135.5 1.0
O2A F:AGS801 2.2 135.5 1.0
OG1 F:THR252 2.3 109.5 1.0
O1B F:AGS801 2.9 135.5 1.0
CB F:THR252 3.0 109.5 1.0
PA F:AGS801 3.3 135.5 1.0
PG F:AGS801 3.5 135.5 1.0
O1A F:AGS801 3.5 135.5 1.0
OD1 F:ASP304 3.5 117.6 1.0
CG2 F:THR252 3.8 109.5 1.0
OD2 F:ASP304 3.8 117.6 1.0
PB F:AGS801 3.9 135.5 1.0
O2G F:AGS801 3.9 135.5 1.0
CG F:ASP304 4.1 117.6 1.0
O3A F:AGS801 4.1 135.5 1.0
O3B F:AGS801 4.2 135.5 1.0
CA F:THR252 4.3 109.5 1.0
N F:THR252 4.4 109.5 1.0
O5' F:AGS801 4.6 135.5 1.0
S1G F:AGS801 4.9 135.5 1.0

Magnesium binding site 7 out of 12 in 7rlj

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Magnesium binding site 7 out of 12 in the Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Mg802

b:164.5
occ:1.00
 O3G L:AGS801 2.1 152.5 1.0
O2A L:AGS801 2.2 152.5 1.0
OG1 L:THR252 2.3 126.2 1.0
O1B L:AGS801 2.9 152.5 1.0
CB L:THR252 3.0 126.2 1.0
PA L:AGS801 3.3 152.5 1.0
PG L:AGS801 3.5 152.5 1.0
O1A L:AGS801 3.5 152.5 1.0
OD1 L:ASP304 3.5 121.7 1.0
CG2 L:THR252 3.8 126.2 1.0
OD2 L:ASP304 3.8 121.7 1.0
PB L:AGS801 3.9 152.5 1.0
O2G L:AGS801 3.9 152.5 1.0
CG L:ASP304 4.1 121.7 1.0
O3A L:AGS801 4.1 152.5 1.0
O3B L:AGS801 4.2 152.5 1.0
CA L:THR252 4.3 126.2 1.0
N L:THR252 4.4 126.2 1.0
O5' L:AGS801 4.6 152.5 1.0
S1G L:AGS801 4.9 152.5 1.0

Magnesium binding site 8 out of 12 in 7rlj

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Magnesium binding site 8 out of 12 in the Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg802

b:128.8
occ:1.00
 O3G G:AGS801 2.1 152.5 1.0
O2A G:AGS801 2.2 152.5 1.0
OG1 G:THR252 2.3 116.1 1.0
O1B G:AGS801 2.9 152.5 1.0
CB G:THR252 3.0 116.1 1.0
PA G:AGS801 3.3 152.5 1.0
PG G:AGS801 3.5 152.5 1.0
O1A G:AGS801 3.5 152.5 1.0
OD1 G:ASP304 3.5 121.8 1.0
CG2 G:THR252 3.8 116.1 1.0
OD2 G:ASP304 3.8 121.8 1.0
PB G:AGS801 3.9 152.5 1.0
O2G G:AGS801 3.9 152.5 1.0
CG G:ASP304 4.1 121.8 1.0
O3A G:AGS801 4.1 152.5 1.0
O3B G:AGS801 4.2 152.5 1.0
CA G:THR252 4.3 116.1 1.0
N G:THR252 4.4 116.1 1.0
O5' G:AGS801 4.6 152.5 1.0
S1G G:AGS801 4.9 152.5 1.0

Magnesium binding site 9 out of 12 in 7rlj

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Magnesium binding site 9 out of 12 in the Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg802

b:113.5
occ:1.00
 O3G H:AGS801 2.1 136.7 1.0
O2A H:AGS801 2.2 136.7 1.0
OG1 H:THR252 2.3 109.2 1.0
O1B H:AGS801 2.9 136.7 1.0
CB H:THR252 3.0 109.2 1.0
PA H:AGS801 3.3 136.7 1.0
PG H:AGS801 3.5 136.7 1.0
O1A H:AGS801 3.5 136.7 1.0
OD1 H:ASP304 3.5 124.5 1.0
CG2 H:THR252 3.8 109.2 1.0
OD2 H:ASP304 3.8 124.5 1.0
PB H:AGS801 3.9 136.7 1.0
O2G H:AGS801 3.9 136.7 1.0
CG H:ASP304 4.1 124.5 1.0
O3A H:AGS801 4.1 136.7 1.0
O3B H:AGS801 4.2 136.7 1.0
CA H:THR252 4.3 109.2 1.0
N H:THR252 4.4 109.2 1.0
O5' H:AGS801 4.6 136.7 1.0
S1G H:AGS801 4.9 136.7 1.0

Magnesium binding site 10 out of 12 in 7rlj

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Magnesium binding site 10 out of 12 in the Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Cryo-Em Structure of Human P97 Bound to Cb-5083 and Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mg802

b:117.8
occ:1.00
 O3G I:AGS801 2.1 103.4 1.0
O2A I:AGS801 2.2 103.4 1.0
OG1 I:THR252 2.3 111.1 1.0
O1B I:AGS801 2.9 103.4 1.0
CB I:THR252 3.0 111.1 1.0
PA I:AGS801 3.3 103.4 1.0
PG I:AGS801 3.5 103.4 1.0
O1A I:AGS801 3.5 103.4 1.0
OD1 I:ASP304 3.5 121.3 1.0
CG2 I:THR252 3.8 111.1 1.0
OD2 I:ASP304 3.8 121.3 1.0
PB I:AGS801 3.9 103.4 1.0
O2G I:AGS801 3.9 103.4 1.0
CG I:ASP304 4.1 121.3 1.0
O3A I:AGS801 4.1 103.4 1.0
O3B I:AGS801 4.2 103.4 1.0
CA I:THR252 4.3 111.1 1.0
N I:THR252 4.4 111.1 1.0
O5' I:AGS801 4.6 103.4 1.0
S1G I:AGS801 4.9 103.4 1.0

Reference:

B.Caffrey, X.Zhu, A.Berezuk, K.Tuttle, S.Chittori, S.Subramaniam. Common Mutations of Aaa Atpase P97 and Inhibitor Binding Disrupt Inter-Domain Coupling and Subsequent Allosteric Activation J.Biol.Chem. 2021.
ISSN: ESSN 1083-351X
DOI: 10.1016/J.JBC.2021.101187
Page generated: Thu Oct 3 07:59:55 2024

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