Magnesium in PDB 6wrf: Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex
Enzymatic activity of Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex
All present enzymatic activity of Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex:
3.4.21.92;
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex
(pdb code 6wrf). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the
Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex, PDB code: 6wrf:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
Magnesium binding site 1 out
of 5 in 6wrf
Go back to
Magnesium Binding Sites List in 6wrf
Magnesium binding site 1 out
of 5 in the Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg502
b:30.0
occ:1.00
|
HG1
|
B:THR126
|
1.6
|
33.8
|
1.0
|
OG1
|
B:THR126
|
2.0
|
33.8
|
1.0
|
O2G
|
B:AGS501
|
2.0
|
32.0
|
1.0
|
O2B
|
B:AGS501
|
2.0
|
32.0
|
1.0
|
OD2
|
B:ASP184
|
3.0
|
28.2
|
1.0
|
PG
|
B:AGS501
|
3.1
|
32.0
|
1.0
|
S1G
|
B:AGS501
|
3.4
|
32.0
|
1.0
|
PB
|
B:AGS501
|
3.4
|
32.0
|
1.0
|
CB
|
B:THR126
|
3.4
|
33.8
|
1.0
|
OD1
|
B:ASP184
|
3.4
|
28.2
|
1.0
|
H
|
B:THR126
|
3.5
|
33.8
|
1.0
|
CG
|
B:ASP184
|
3.6
|
28.2
|
1.0
|
HB
|
B:THR126
|
3.7
|
33.8
|
1.0
|
O3B
|
B:AGS501
|
3.7
|
32.0
|
1.0
|
HE2
|
B:LYS125
|
3.8
|
26.4
|
1.0
|
HH22
|
C:ARG307
|
3.8
|
27.9
|
1.0
|
HG21
|
B:THR126
|
3.9
|
33.8
|
1.0
|
HB2
|
B:LYS125
|
4.0
|
26.4
|
1.0
|
O1B
|
B:AGS501
|
4.1
|
32.0
|
1.0
|
HH
|
B:TYR182
|
4.1
|
27.3
|
1.0
|
CG2
|
B:THR126
|
4.1
|
33.8
|
1.0
|
N
|
B:THR126
|
4.1
|
33.8
|
1.0
|
OE2
|
B:GLU185
|
4.1
|
30.3
|
1.0
|
O1A
|
B:AGS501
|
4.2
|
32.0
|
1.0
|
HG23
|
B:THR126
|
4.3
|
33.8
|
1.0
|
CA
|
B:THR126
|
4.3
|
33.8
|
1.0
|
O3G
|
B:AGS501
|
4.4
|
32.0
|
1.0
|
O3A
|
B:AGS501
|
4.5
|
32.0
|
1.0
|
HA
|
B:THR126
|
4.5
|
33.8
|
1.0
|
HH12
|
C:ARG307
|
4.5
|
27.9
|
1.0
|
OE1
|
C:GLU216
|
4.6
|
30.7
|
1.0
|
OH
|
B:TYR182
|
4.6
|
27.3
|
1.0
|
NH2
|
C:ARG307
|
4.7
|
27.9
|
1.0
|
HH11
|
B:ARG370
|
4.7
|
30.4
|
1.0
|
CE
|
B:LYS125
|
4.7
|
26.4
|
1.0
|
HD3
|
C:LYS213
|
4.7
|
31.4
|
1.0
|
HZ3
|
B:LYS125
|
4.7
|
26.4
|
1.0
|
HZ1
|
B:LYS125
|
4.8
|
26.4
|
1.0
|
PA
|
B:AGS501
|
4.8
|
32.0
|
1.0
|
CD
|
B:GLU185
|
5.0
|
30.3
|
1.0
|
CB
|
B:LYS125
|
5.0
|
26.4
|
1.0
|
HD2
|
C:LYS213
|
5.0
|
31.4
|
1.0
|
HH12
|
B:ARG370
|
5.0
|
30.4
|
1.0
|
NZ
|
B:LYS125
|
5.0
|
26.4
|
1.0
|
|
Magnesium binding site 2 out
of 5 in 6wrf
Go back to
Magnesium Binding Sites List in 6wrf
Magnesium binding site 2 out
of 5 in the Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg502
b:30.0
occ:1.00
|
HG1
|
C:THR126
|
1.6
|
39.9
|
1.0
|
OG1
|
C:THR126
|
2.0
|
39.9
|
1.0
|
O2G
|
C:AGS501
|
2.0
|
47.0
|
1.0
|
O2B
|
C:AGS501
|
2.4
|
47.0
|
1.0
|
OD2
|
C:ASP184
|
2.4
|
27.9
|
1.0
|
CG
|
C:ASP184
|
3.2
|
27.9
|
1.0
|
OD1
|
C:ASP184
|
3.2
|
27.9
|
1.0
|
CB
|
C:THR126
|
3.4
|
39.9
|
1.0
|
PG
|
C:AGS501
|
3.5
|
47.0
|
1.0
|
H
|
C:THR126
|
3.7
|
39.9
|
1.0
|
HG21
|
C:THR126
|
3.7
|
39.9
|
1.0
|
HB
|
C:THR126
|
3.7
|
39.9
|
1.0
|
PB
|
C:AGS501
|
3.8
|
47.0
|
1.0
|
CG2
|
C:THR126
|
4.0
|
39.9
|
1.0
|
OE2
|
C:GLU185
|
4.0
|
28.8
|
1.0
|
O3B
|
C:AGS501
|
4.1
|
47.0
|
1.0
|
HG23
|
C:THR126
|
4.1
|
39.9
|
1.0
|
HE2
|
C:LYS125
|
4.1
|
26.9
|
1.0
|
HH12
|
D:ARG307
|
4.2
|
28.9
|
1.0
|
HB2
|
C:LYS125
|
4.2
|
26.9
|
1.0
|
N
|
C:THR126
|
4.3
|
39.9
|
1.0
|
HH
|
C:TYR182
|
4.3
|
26.3
|
1.0
|
CA
|
C:THR126
|
4.3
|
39.9
|
1.0
|
HH22
|
D:ARG307
|
4.4
|
28.9
|
1.0
|
S1G
|
C:AGS501
|
4.4
|
47.0
|
1.0
|
HZ2
|
D:LYS213
|
4.4
|
31.3
|
1.0
|
O3G
|
C:AGS501
|
4.5
|
47.0
|
1.0
|
HA
|
C:THR126
|
4.5
|
39.9
|
1.0
|
HZ3
|
D:LYS213
|
4.6
|
31.3
|
1.0
|
CB
|
C:ASP184
|
4.6
|
27.9
|
1.0
|
O1A
|
C:AGS501
|
4.6
|
47.0
|
1.0
|
O1B
|
C:AGS501
|
4.7
|
47.0
|
1.0
|
HG2
|
C:GLU185
|
4.7
|
28.8
|
1.0
|
CD
|
C:GLU185
|
4.7
|
28.8
|
1.0
|
O3A
|
C:AGS501
|
4.7
|
47.0
|
1.0
|
OH
|
C:TYR182
|
4.8
|
26.3
|
1.0
|
HE2
|
C:TYR182
|
4.8
|
26.3
|
1.0
|
HH12
|
C:ARG370
|
4.8
|
32.0
|
1.0
|
H
|
C:GLU185
|
4.8
|
28.8
|
1.0
|
HB3
|
C:ASP184
|
4.8
|
27.9
|
1.0
|
HG22
|
C:THR126
|
4.9
|
39.9
|
1.0
|
NZ
|
D:LYS213
|
4.9
|
31.3
|
1.0
|
HB2
|
C:ASP184
|
4.9
|
27.9
|
1.0
|
NH1
|
D:ARG307
|
5.0
|
28.9
|
1.0
|
|
Magnesium binding site 3 out
of 5 in 6wrf
Go back to
Magnesium Binding Sites List in 6wrf
Magnesium binding site 3 out
of 5 in the Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg502
b:30.0
occ:1.00
|
HG1
|
D:THR126
|
1.6
|
34.6
|
1.0
|
OG1
|
D:THR126
|
2.0
|
34.6
|
1.0
|
O2G
|
D:AGS501
|
2.0
|
47.0
|
1.0
|
O2B
|
D:AGS501
|
2.5
|
47.0
|
1.0
|
OD2
|
D:ASP184
|
2.6
|
29.5
|
1.0
|
OD1
|
D:ASP184
|
3.2
|
29.5
|
1.0
|
CG
|
D:ASP184
|
3.3
|
29.5
|
1.0
|
CB
|
D:THR126
|
3.4
|
34.6
|
1.0
|
PG
|
D:AGS501
|
3.5
|
47.0
|
1.0
|
HG21
|
D:THR126
|
3.7
|
34.6
|
1.0
|
H
|
D:THR126
|
3.8
|
34.6
|
1.0
|
HB
|
D:THR126
|
3.8
|
34.6
|
1.0
|
PB
|
D:AGS501
|
3.9
|
47.0
|
1.0
|
OE2
|
D:GLU185
|
3.9
|
30.6
|
1.0
|
CG2
|
D:THR126
|
4.0
|
34.6
|
1.0
|
HG23
|
D:THR126
|
4.0
|
34.6
|
1.0
|
OE1
|
E:GLU216
|
4.1
|
34.8
|
1.0
|
HE2
|
D:LYS125
|
4.2
|
28.9
|
1.0
|
O3B
|
D:AGS501
|
4.2
|
47.0
|
1.0
|
HH22
|
E:ARG307
|
4.3
|
30.7
|
1.0
|
HD3
|
E:LYS213
|
4.3
|
32.9
|
1.0
|
HB2
|
D:LYS125
|
4.3
|
28.9
|
1.0
|
N
|
D:THR126
|
4.3
|
34.6
|
1.0
|
CA
|
D:THR126
|
4.3
|
34.6
|
1.0
|
HH21
|
E:ARG307
|
4.4
|
30.7
|
1.0
|
OE2
|
E:GLU216
|
4.4
|
34.8
|
1.0
|
O3G
|
D:AGS501
|
4.5
|
47.0
|
1.0
|
S1G
|
D:AGS501
|
4.5
|
47.0
|
1.0
|
HA
|
D:THR126
|
4.5
|
34.6
|
1.0
|
O1A
|
D:AGS501
|
4.5
|
47.0
|
1.0
|
O1B
|
D:AGS501
|
4.6
|
47.0
|
1.0
|
NH2
|
E:ARG307
|
4.6
|
30.7
|
1.0
|
CD
|
D:GLU185
|
4.6
|
30.6
|
1.0
|
OH
|
D:TYR182
|
4.6
|
24.8
|
1.0
|
CD
|
E:GLU216
|
4.7
|
34.8
|
1.0
|
HH12
|
D:ARG370
|
4.7
|
26.7
|
1.0
|
CB
|
D:ASP184
|
4.7
|
29.5
|
1.0
|
H
|
D:GLU185
|
4.7
|
30.6
|
1.0
|
HG2
|
D:GLU185
|
4.9
|
30.6
|
1.0
|
HG22
|
D:THR126
|
4.9
|
34.6
|
1.0
|
O3A
|
D:AGS501
|
4.9
|
47.0
|
1.0
|
HE2
|
D:TYR182
|
5.0
|
24.8
|
1.0
|
HB3
|
D:ASP184
|
5.0
|
29.5
|
1.0
|
HH
|
D:TYR182
|
5.0
|
24.8
|
1.0
|
HZ3
|
D:LYS125
|
5.0
|
28.9
|
1.0
|
|
Magnesium binding site 4 out
of 5 in 6wrf
Go back to
Magnesium Binding Sites List in 6wrf
Magnesium binding site 4 out
of 5 in the Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg502
b:30.0
occ:1.00
|
O2G
|
E:AGS501
|
2.0
|
46.9
|
1.0
|
OD2
|
E:ASP184
|
2.0
|
38.9
|
1.0
|
OD1
|
E:ASP184
|
2.1
|
38.9
|
1.0
|
CG
|
E:ASP184
|
2.3
|
38.9
|
1.0
|
HG1
|
E:THR126
|
2.7
|
37.7
|
1.0
|
OG1
|
E:THR126
|
3.1
|
37.7
|
1.0
|
PG
|
E:AGS501
|
3.3
|
46.9
|
1.0
|
O2B
|
E:AGS501
|
3.3
|
46.9
|
1.0
|
HE2
|
E:LYS125
|
3.3
|
36.6
|
1.0
|
HH
|
E:TYR182
|
3.4
|
33.2
|
1.0
|
S1G
|
E:AGS501
|
3.6
|
46.9
|
1.0
|
H
|
E:GLU185
|
3.8
|
42.4
|
1.0
|
CB
|
E:ASP184
|
3.9
|
38.9
|
1.0
|
OH
|
E:TYR182
|
4.1
|
33.2
|
1.0
|
HB2
|
E:LYS125
|
4.1
|
36.6
|
1.0
|
O3B
|
E:AGS501
|
4.1
|
46.9
|
1.0
|
HG2
|
E:GLU185
|
4.2
|
42.4
|
1.0
|
HB2
|
E:ASP184
|
4.2
|
38.9
|
1.0
|
CE
|
E:LYS125
|
4.2
|
36.6
|
1.0
|
HE2
|
E:TYR182
|
4.2
|
33.2
|
1.0
|
H
|
E:THR126
|
4.3
|
37.7
|
1.0
|
HB3
|
E:ASP184
|
4.3
|
38.9
|
1.0
|
OE1
|
E:GLU185
|
4.3
|
42.4
|
1.0
|
PB
|
E:AGS501
|
4.3
|
46.9
|
1.0
|
O3G
|
E:AGS501
|
4.4
|
46.9
|
1.0
|
HA
|
E:ASP184
|
4.4
|
38.9
|
1.0
|
CD
|
E:GLU185
|
4.5
|
42.4
|
1.0
|
CB
|
E:THR126
|
4.5
|
37.7
|
1.0
|
N
|
E:GLU185
|
4.5
|
42.4
|
1.0
|
HE3
|
E:LYS125
|
4.5
|
36.6
|
1.0
|
HZ3
|
E:LYS125
|
4.6
|
36.6
|
1.0
|
HB3
|
E:LYS125
|
4.7
|
36.6
|
1.0
|
CA
|
E:ASP184
|
4.7
|
38.9
|
1.0
|
HZ2
|
E:LYS125
|
4.8
|
36.6
|
1.0
|
N
|
E:THR126
|
4.8
|
37.7
|
1.0
|
HB
|
E:THR126
|
4.8
|
37.7
|
1.0
|
NZ
|
E:LYS125
|
4.8
|
36.6
|
1.0
|
O
|
E:GLY248
|
4.8
|
31.3
|
1.0
|
CG
|
E:GLU185
|
4.8
|
42.4
|
1.0
|
CB
|
E:LYS125
|
4.8
|
36.6
|
1.0
|
OE2
|
E:GLU185
|
4.9
|
42.4
|
1.0
|
O1B
|
E:AGS501
|
5.0
|
46.9
|
1.0
|
CE2
|
E:TYR182
|
5.0
|
33.2
|
1.0
|
|
Magnesium binding site 5 out
of 5 in 6wrf
Go back to
Magnesium Binding Sites List in 6wrf
Magnesium binding site 5 out
of 5 in the Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex
Mono view
Stereo pair view
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A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Clpx-Clpp Complex Bound to Gfp-Ssra, Recognition Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg502
b:30.0
occ:1.00
|
OD2
|
A:ASP184
|
2.0
|
44.6
|
1.0
|
HG1
|
A:THR126
|
2.0
|
42.1
|
1.0
|
OG1
|
A:THR126
|
2.0
|
42.1
|
1.0
|
OD1
|
A:ASP184
|
2.3
|
44.6
|
1.0
|
S1G
|
A:AGS501
|
2.4
|
43.7
|
1.0
|
CG
|
A:ASP184
|
2.4
|
44.6
|
1.0
|
O2B
|
A:AGS501
|
3.3
|
43.7
|
1.0
|
CB
|
A:THR126
|
3.4
|
42.1
|
1.0
|
OH
|
A:TYR182
|
3.5
|
48.0
|
1.0
|
HH
|
A:TYR182
|
3.7
|
48.0
|
1.0
|
H
|
A:THR126
|
3.7
|
42.1
|
1.0
|
HG21
|
A:THR126
|
3.7
|
42.1
|
1.0
|
OE2
|
A:GLU185
|
3.8
|
42.2
|
1.0
|
HE2
|
A:LYS125
|
3.9
|
38.2
|
1.0
|
CG2
|
A:THR126
|
3.9
|
42.1
|
1.0
|
CB
|
A:ASP184
|
3.9
|
44.6
|
1.0
|
HG23
|
A:THR126
|
3.9
|
42.1
|
1.0
|
HB
|
A:THR126
|
4.0
|
42.1
|
1.0
|
N
|
A:THR126
|
4.0
|
42.1
|
1.0
|
HB2
|
A:LYS125
|
4.0
|
38.2
|
1.0
|
HA
|
A:THR126
|
4.1
|
42.1
|
1.0
|
CA
|
A:THR126
|
4.1
|
42.1
|
1.0
|
HB3
|
A:LYS125
|
4.2
|
38.2
|
1.0
|
PG
|
A:AGS501
|
4.2
|
43.7
|
1.0
|
HB2
|
A:ASP184
|
4.3
|
44.6
|
1.0
|
HB3
|
A:ASP184
|
4.3
|
44.6
|
1.0
|
H
|
A:GLU185
|
4.3
|
42.2
|
1.0
|
CD
|
A:GLU185
|
4.3
|
42.2
|
1.0
|
PB
|
A:AGS501
|
4.5
|
43.7
|
1.0
|
HG2
|
A:GLU185
|
4.5
|
42.2
|
1.0
|
HE2
|
A:TYR182
|
4.5
|
48.0
|
1.0
|
CB
|
A:LYS125
|
4.6
|
38.2
|
1.0
|
HA
|
A:ASP184
|
4.6
|
44.6
|
1.0
|
O1B
|
A:AGS501
|
4.6
|
43.7
|
1.0
|
CZ
|
A:TYR182
|
4.7
|
48.0
|
1.0
|
HA2
|
A:GLY249
|
4.7
|
42.5
|
1.0
|
O3G
|
A:AGS501
|
4.8
|
43.7
|
1.0
|
OE1
|
A:GLU185
|
4.8
|
42.2
|
1.0
|
CE
|
A:LYS125
|
4.9
|
38.2
|
1.0
|
CA
|
A:ASP184
|
4.9
|
44.6
|
1.0
|
HG22
|
A:THR126
|
4.9
|
42.1
|
1.0
|
C
|
A:LYS125
|
4.9
|
38.2
|
1.0
|
O3B
|
A:AGS501
|
4.9
|
43.7
|
1.0
|
N
|
A:GLU185
|
4.9
|
42.2
|
1.0
|
|
Reference:
X.Fei,
T.A.Bell,
S.R.Barkow,
T.A.Baker,
R.T.Sauer.
Structural Basis of Clpxp Recognition and Unfolding of Ssra-Tagged Substrates. Elife V. 9 2020.
ISSN: ESSN 2050-084X
PubMed: 33089779
DOI: 10.7554/ELIFE.61496
Page generated: Tue Oct 1 23:10:55 2024
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