Magnesium in PDB 7rla: Cryo-Em Structure of Human P97-R191Q Mutant Bound to Atpgs.

Enzymatic activity of Cryo-Em Structure of Human P97-R191Q Mutant Bound to Atpgs.

All present enzymatic activity of Cryo-Em Structure of Human P97-R191Q Mutant Bound to 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-R191Q Mutant Bound to Atpgs. (pdb code 7rla). 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-R191Q Mutant Bound to Atpgs., PDB code: 7rla:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 12 in 7rla

Go back to Magnesium Binding Sites List in 7rla
Magnesium binding site 1 out of 12 in the Cryo-Em Structure of Human P97-R191Q Mutant Bound to 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-R191Q Mutant Bound to Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg903

b:121.5
occ:1.00
 O1A A:AGS902 2.1 126.1 1.0
O2G A:AGS902 2.1 126.1 1.0
O1B A:AGS902 2.1 126.1 1.0
OG1 A:THR525 2.3 116.3 1.0
PB A:AGS902 3.1 126.1 1.0
PA A:AGS902 3.1 126.1 1.0
O3A A:AGS902 3.3 126.1 1.0
PG A:AGS902 3.4 126.1 1.0
CB A:THR525 3.5 116.3 1.0
OD2 A:ASP577 3.5 117.0 1.0
O3B A:AGS902 3.6 126.1 1.0
O2A A:AGS902 3.8 126.1 1.0
OD1 A:ASP577 4.2 117.0 1.0
CG A:ASP577 4.3 117.0 1.0
N A:THR525 4.3 116.3 1.0
O5' A:AGS902 4.4 126.1 1.0
CG2 A:THR525 4.4 116.3 1.0
O2B A:AGS902 4.5 126.1 1.0
NH1 F:ARG635 4.5 119.0 1.0
S1G A:AGS902 4.5 126.1 1.0
O3G A:AGS902 4.5 126.1 1.0
CA A:THR525 4.5 116.3 1.0
C5' A:AGS902 4.8 126.1 1.0

Magnesium binding site 2 out of 12 in 7rla

Go back to Magnesium Binding Sites List in 7rla
Magnesium binding site 2 out of 12 in the Cryo-Em Structure of Human P97-R191Q Mutant Bound to 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-R191Q Mutant Bound to Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg904

b:130.3
occ:1.00
 O2G A:AGS901 2.3 137.6 1.0
OG1 A:THR252 2.8 125.1 1.0
O3G A:AGS901 3.2 137.6 1.0
PG A:AGS901 3.3 137.6 1.0
O1B A:AGS901 3.4 137.6 1.0
OD1 A:ASP304 3.4 123.8 1.0
OD2 A:ASP304 3.6 123.8 1.0
CG A:ASP304 3.9 123.8 1.0
O3B A:AGS901 4.0 137.6 1.0
CB A:THR252 4.1 125.1 1.0
PB A:AGS901 4.3 137.6 1.0
O1A A:AGS901 4.4 137.6 1.0
CG A:GLU305 4.5 127.7 1.0
OE2 A:GLU305 4.5 127.7 1.0
N A:THR252 4.8 125.1 1.0
CD A:GLU305 4.9 127.7 1.0
S1G A:AGS901 4.9 137.6 1.0

Magnesium binding site 3 out of 12 in 7rla

Go back to Magnesium Binding Sites List in 7rla
Magnesium binding site 3 out of 12 in the Cryo-Em Structure of Human P97-R191Q Mutant Bound to 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-R191Q Mutant Bound to Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg903

b:120.1
occ:1.00
 O1A B:AGS902 2.1 122.6 1.0
O2G B:AGS902 2.1 122.6 1.0
O1B B:AGS902 2.1 122.6 1.0
OG1 B:THR525 2.3 114.5 1.0
PB B:AGS902 3.1 122.6 1.0
PA B:AGS902 3.1 122.6 1.0
O3A B:AGS902 3.3 122.6 1.0
PG B:AGS902 3.4 122.6 1.0
CB B:THR525 3.5 114.5 1.0
OD2 B:ASP577 3.5 115.6 1.0
O3B B:AGS902 3.6 122.6 1.0
O2A B:AGS902 3.8 122.6 1.0
OD1 B:ASP577 4.2 115.6 1.0
CG B:ASP577 4.3 115.6 1.0
N B:THR525 4.3 114.5 1.0
O5' B:AGS902 4.4 122.6 1.0
CG2 B:THR525 4.4 114.5 1.0
O2B B:AGS902 4.5 122.6 1.0
S1G B:AGS902 4.5 122.6 1.0
O3G B:AGS902 4.5 122.6 1.0
CA B:THR525 4.5 114.5 1.0
NH1 A:ARG635 4.6 121.1 1.0
C5' B:AGS902 4.8 122.6 1.0

Magnesium binding site 4 out of 12 in 7rla

Go back to Magnesium Binding Sites List in 7rla
Magnesium binding site 4 out of 12 in the Cryo-Em Structure of Human P97-R191Q Mutant Bound to 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-R191Q Mutant Bound to Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg904

b:129.1
occ:1.00
 O2G B:AGS901 2.3 135.0 1.0
OG1 B:THR252 2.8 124.8 1.0
O3G B:AGS901 3.2 135.0 1.0
PG B:AGS901 3.3 135.0 1.0
O1B B:AGS901 3.4 135.0 1.0
OD1 B:ASP304 3.4 125.4 1.0
OD2 B:ASP304 3.6 125.4 1.0
CG B:ASP304 3.9 125.4 1.0
O3B B:AGS901 4.0 135.0 1.0
CB B:THR252 4.1 124.8 1.0
PB B:AGS901 4.3 135.0 1.0
O1A B:AGS901 4.4 135.0 1.0
CG B:GLU305 4.5 129.3 1.0
OE2 B:GLU305 4.5 129.3 1.0
N B:THR252 4.8 124.8 1.0
CD B:GLU305 4.9 129.3 1.0
S1G B:AGS901 4.9 135.0 1.0

Magnesium binding site 5 out of 12 in 7rla

Go back to Magnesium Binding Sites List in 7rla
Magnesium binding site 5 out of 12 in the Cryo-Em Structure of Human P97-R191Q Mutant Bound to 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-R191Q Mutant Bound to Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg903

b:119.5
occ:1.00
 O1A C:AGS902 2.1 122.5 1.0
O2G C:AGS902 2.1 122.5 1.0
O1B C:AGS902 2.1 122.5 1.0
OG1 C:THR525 2.3 116.8 1.0
PB C:AGS902 3.1 122.5 1.0
PA C:AGS902 3.1 122.5 1.0
O3A C:AGS902 3.3 122.5 1.0
PG C:AGS902 3.4 122.5 1.0
CB C:THR525 3.5 116.8 1.0
OD2 C:ASP577 3.5 119.9 1.0
O3B C:AGS902 3.6 122.5 1.0
O2A C:AGS902 3.8 122.5 1.0
OD1 C:ASP577 4.2 119.9 1.0
CG C:ASP577 4.3 119.9 1.0
N C:THR525 4.3 116.8 1.0
O5' C:AGS902 4.4 122.5 1.0
CG2 C:THR525 4.4 116.8 1.0
O2B C:AGS902 4.5 122.5 1.0
S1G C:AGS902 4.5 122.5 1.0
O3G C:AGS902 4.5 122.5 1.0
CA C:THR525 4.5 116.8 1.0
NH1 B:ARG635 4.7 120.5 1.0
C5' C:AGS902 4.8 122.5 1.0

Magnesium binding site 6 out of 12 in 7rla

Go back to Magnesium Binding Sites List in 7rla
Magnesium binding site 6 out of 12 in the Cryo-Em Structure of Human P97-R191Q Mutant Bound to 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-R191Q Mutant Bound to Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg904

b:128.3
occ:1.00
 O2G C:AGS901 2.3 137.7 1.0
OG1 C:THR252 2.8 129.0 1.0
O3G C:AGS901 3.2 137.7 1.0
PG C:AGS901 3.3 137.7 1.0
O1B C:AGS901 3.4 137.7 1.0
OD1 C:ASP304 3.4 130.0 1.0
OD2 C:ASP304 3.6 130.0 1.0
CG C:ASP304 3.9 130.0 1.0
O3B C:AGS901 4.0 137.7 1.0
CB C:THR252 4.1 129.0 1.0
PB C:AGS901 4.3 137.7 1.0
O1A C:AGS901 4.4 137.7 1.0
CG C:GLU305 4.5 132.2 1.0
OE2 C:GLU305 4.5 132.2 1.0
N C:THR252 4.8 129.0 1.0
CD C:GLU305 4.9 132.2 1.0
S1G C:AGS901 4.9 137.7 1.0

Magnesium binding site 7 out of 12 in 7rla

Go back to Magnesium Binding Sites List in 7rla
Magnesium binding site 7 out of 12 in the Cryo-Em Structure of Human P97-R191Q Mutant Bound to 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-R191Q Mutant Bound to Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg903

b:119.5
occ:1.00
 O1A D:AGS902 2.1 123.5 1.0
O2G D:AGS902 2.1 123.5 1.0
O1B D:AGS902 2.1 123.5 1.0
OG1 D:THR525 2.3 114.2 1.0
PB D:AGS902 3.1 123.5 1.0
PA D:AGS902 3.1 123.5 1.0
O3A D:AGS902 3.3 123.5 1.0
PG D:AGS902 3.4 123.5 1.0
CB D:THR525 3.5 114.2 1.0
OD2 D:ASP577 3.5 116.2 1.0
O3B D:AGS902 3.6 123.5 1.0
O2A D:AGS902 3.8 123.5 1.0
OD1 D:ASP577 4.2 116.2 1.0
CG D:ASP577 4.3 116.2 1.0
N D:THR525 4.3 114.2 1.0
O5' D:AGS902 4.4 123.5 1.0
CG2 D:THR525 4.4 114.2 1.0
O2B D:AGS902 4.5 123.5 1.0
S1G D:AGS902 4.5 123.5 1.0
O3G D:AGS902 4.5 123.5 1.0
CA D:THR525 4.5 114.2 1.0
NH1 C:ARG635 4.7 121.8 1.0
C5' D:AGS902 4.8 123.5 1.0

Magnesium binding site 8 out of 12 in 7rla

Go back to Magnesium Binding Sites List in 7rla
Magnesium binding site 8 out of 12 in the Cryo-Em Structure of Human P97-R191Q Mutant Bound to 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-R191Q Mutant Bound to Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg904

b:127.6
occ:1.00
 O2G D:AGS901 2.3 137.9 1.0
OG1 D:THR252 2.8 125.3 1.0
O3G D:AGS901 3.2 137.9 1.0
PG D:AGS901 3.3 137.9 1.0
O1B D:AGS901 3.4 137.9 1.0
OD1 D:ASP304 3.4 124.0 1.0
OD2 D:ASP304 3.6 124.0 1.0
CG D:ASP304 3.9 124.0 1.0
O3B D:AGS901 4.0 137.9 1.0
CB D:THR252 4.1 125.3 1.0
PB D:AGS901 4.3 137.9 1.0
O1A D:AGS901 4.4 137.9 1.0
CG D:GLU305 4.5 127.4 1.0
OE2 D:GLU305 4.5 127.4 1.0
N D:THR252 4.8 125.3 1.0
CD D:GLU305 4.9 127.4 1.0
S1G D:AGS901 4.9 137.9 1.0

Magnesium binding site 9 out of 12 in 7rla

Go back to Magnesium Binding Sites List in 7rla
Magnesium binding site 9 out of 12 in the Cryo-Em Structure of Human P97-R191Q Mutant Bound to 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-R191Q Mutant Bound to Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg903

b:117.2
occ:1.00
 O1A E:AGS902 2.1 122.9 1.0
O2G E:AGS902 2.1 122.9 1.0
O1B E:AGS902 2.1 122.9 1.0
OG1 E:THR525 2.3 114.6 1.0
PB E:AGS902 3.1 122.9 1.0
PA E:AGS902 3.1 122.9 1.0
O3A E:AGS902 3.3 122.9 1.0
PG E:AGS902 3.4 122.9 1.0
CB E:THR525 3.5 114.6 1.0
OD2 E:ASP577 3.5 117.3 1.0
O3B E:AGS902 3.6 122.9 1.0
O2A E:AGS902 3.8 122.9 1.0
OD1 E:ASP577 4.2 117.3 1.0
CG E:ASP577 4.3 117.3 1.0
N E:THR525 4.3 114.6 1.0
O5' E:AGS902 4.4 122.9 1.0
CG2 E:THR525 4.4 114.6 1.0
O2B E:AGS902 4.5 122.9 1.0
S1G E:AGS902 4.5 122.9 1.0
O3G E:AGS902 4.5 122.9 1.0
CA E:THR525 4.5 114.6 1.0
NH1 D:ARG635 4.6 122.0 1.0
C5' E:AGS902 4.8 122.9 1.0

Magnesium binding site 10 out of 12 in 7rla

Go back to Magnesium Binding Sites List in 7rla
Magnesium binding site 10 out of 12 in the Cryo-Em Structure of Human P97-R191Q Mutant Bound to 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-R191Q Mutant Bound to Atpgs. within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg904

b:129.0
occ:1.00
 O2G E:AGS901 2.3 136.5 1.0
OG1 E:THR252 2.8 127.9 1.0
O3G E:AGS901 3.2 136.5 1.0
PG E:AGS901 3.3 136.5 1.0
O1B E:AGS901 3.4 136.5 1.0
OD1 E:ASP304 3.4 127.4 1.0
OD2 E:ASP304 3.6 127.4 1.0
CG E:ASP304 3.9 127.4 1.0
O3B E:AGS901 4.0 136.5 1.0
CB E:THR252 4.1 127.9 1.0
PB E:AGS901 4.3 136.5 1.0
O1A E:AGS901 4.4 136.5 1.0
CG E:GLU305 4.5 129.5 1.0
OE2 E:GLU305 4.5 129.5 1.0
N E:THR252 4.8 127.9 1.0
CD E:GLU305 4.9 129.5 1.0
S1G E:AGS901 4.9 136.5 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: Fri Sep 24 15:45:36 2021

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy