Magnesium in PDB 7uiy: Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia
Enzymatic activity of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia
All present enzymatic activity of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia:
3.4.21.92;
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia
(pdb code 7uiy). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the
Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia, PDB code: 7uiy:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
Magnesium binding site 1 out
of 5 in 7uiy
Go back to
Magnesium Binding Sites List in 7uiy
Magnesium binding site 1 out
of 5 in the Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg803
b:74.0
occ:1.00
|
HG1
|
A:THR502
|
2.5
|
101.0
|
1.0
|
OG1
|
A:THR502
|
2.6
|
101.0
|
1.0
|
O3G
|
A:AGS802
|
2.8
|
90.7
|
1.0
|
HG1
|
A:THR604
|
3.0
|
111.2
|
1.0
|
O2B
|
A:AGS802
|
3.0
|
90.7
|
1.0
|
OG1
|
A:THR604
|
3.7
|
111.2
|
1.0
|
HH22
|
B:ARG643
|
3.8
|
54.0
|
1.0
|
CB
|
A:THR502
|
3.9
|
101.0
|
1.0
|
HG3
|
A:LYS501
|
4.0
|
99.8
|
1.0
|
HD2
|
A:LYS501
|
4.0
|
99.8
|
1.0
|
HB3
|
A:ASP564
|
4.1
|
112.3
|
1.0
|
HG21
|
A:THR502
|
4.1
|
101.0
|
1.0
|
PG
|
A:AGS802
|
4.2
|
90.7
|
1.0
|
HB
|
A:THR502
|
4.2
|
101.0
|
1.0
|
HB
|
A:THR604
|
4.2
|
111.2
|
1.0
|
OD1
|
A:ASP564
|
4.2
|
112.3
|
1.0
|
PB
|
A:AGS802
|
4.3
|
90.7
|
1.0
|
HG21
|
A:THR604
|
4.4
|
111.2
|
1.0
|
CG
|
A:ASP564
|
4.4
|
112.3
|
1.0
|
O3B
|
A:AGS802
|
4.4
|
90.7
|
1.0
|
NH2
|
B:ARG643
|
4.5
|
54.0
|
1.0
|
HH21
|
B:ARG643
|
4.5
|
54.0
|
1.0
|
CB
|
A:THR604
|
4.5
|
111.2
|
1.0
|
CG2
|
A:THR502
|
4.6
|
101.0
|
1.0
|
H
|
A:THR502
|
4.7
|
101.0
|
1.0
|
OD1
|
A:ASN606
|
4.7
|
101.4
|
1.0
|
CG
|
A:LYS501
|
4.7
|
99.8
|
1.0
|
CB
|
A:ASP564
|
4.7
|
112.3
|
1.0
|
O2A
|
A:AGS802
|
4.8
|
90.7
|
1.0
|
CD
|
A:LYS501
|
4.8
|
99.8
|
1.0
|
HD22
|
A:ASN606
|
4.8
|
101.4
|
1.0
|
HG2
|
A:LYS501
|
4.9
|
99.8
|
1.0
|
O2G
|
A:AGS802
|
4.9
|
90.7
|
1.0
|
HH21
|
A:ARG518
|
4.9
|
108.5
|
1.0
|
HA
|
A:ASP564
|
4.9
|
112.3
|
1.0
|
OD2
|
A:ASP564
|
4.9
|
112.3
|
1.0
|
O3A
|
A:AGS802
|
4.9
|
90.7
|
1.0
|
CG2
|
A:THR604
|
4.9
|
111.2
|
1.0
|
HG23
|
A:THR502
|
5.0
|
101.0
|
1.0
|
CA
|
A:THR502
|
5.0
|
101.0
|
1.0
|
|
Magnesium binding site 2 out
of 5 in 7uiy
Go back to
Magnesium Binding Sites List in 7uiy
Magnesium binding site 2 out
of 5 in the Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg803
b:41.1
occ:1.00
|
O2B
|
B:AGS802
|
2.0
|
34.2
|
1.0
|
OG1
|
B:THR502
|
2.1
|
35.3
|
1.0
|
HG1
|
B:THR604
|
2.8
|
37.8
|
1.0
|
OD2
|
B:ASP564
|
3.0
|
39.6
|
1.0
|
OD1
|
B:ASP564
|
3.2
|
39.6
|
1.0
|
PB
|
B:AGS802
|
3.2
|
34.2
|
1.0
|
CG
|
B:ASP564
|
3.4
|
39.6
|
1.0
|
S1G
|
B:AGS802
|
3.4
|
34.2
|
1.0
|
CB
|
B:THR502
|
3.4
|
35.3
|
1.0
|
OG1
|
B:THR604
|
3.5
|
37.8
|
1.0
|
HB
|
B:THR502
|
3.6
|
35.3
|
1.0
|
O1B
|
B:AGS802
|
3.7
|
34.2
|
1.0
|
H
|
B:THR502
|
3.9
|
35.3
|
1.0
|
HB
|
B:THR604
|
3.9
|
37.8
|
1.0
|
HB2
|
B:LYS501
|
3.9
|
37.2
|
1.0
|
HG21
|
B:THR502
|
3.9
|
35.3
|
1.0
|
O3B
|
B:AGS802
|
4.0
|
34.2
|
1.0
|
HH22
|
C:ARG643
|
4.0
|
29.5
|
1.0
|
HG21
|
B:THR604
|
4.0
|
37.8
|
1.0
|
OE1
|
B:GLU565
|
4.1
|
39.0
|
1.0
|
HD21
|
B:ASN606
|
4.1
|
36.9
|
1.0
|
CB
|
B:THR604
|
4.2
|
37.8
|
1.0
|
N
|
B:THR502
|
4.2
|
35.3
|
1.0
|
PG
|
B:AGS802
|
4.2
|
34.2
|
1.0
|
CG2
|
B:THR502
|
4.3
|
35.3
|
1.0
|
HE3
|
B:LYS501
|
4.3
|
37.2
|
1.0
|
CA
|
B:THR502
|
4.3
|
35.3
|
1.0
|
O3A
|
B:AGS802
|
4.4
|
34.2
|
1.0
|
HA
|
B:THR502
|
4.5
|
35.3
|
1.0
|
O2G
|
B:AGS802
|
4.5
|
34.2
|
1.0
|
CG2
|
B:THR604
|
4.6
|
37.8
|
1.0
|
NH2
|
C:ARG643
|
4.7
|
29.5
|
1.0
|
HB3
|
B:LYS501
|
4.7
|
37.2
|
1.0
|
CB
|
B:LYS501
|
4.7
|
37.2
|
1.0
|
CB
|
B:ASP564
|
4.7
|
39.6
|
1.0
|
HG23
|
B:THR502
|
4.8
|
35.3
|
1.0
|
HH21
|
C:ARG643
|
4.8
|
29.5
|
1.0
|
O2A
|
B:AGS802
|
4.8
|
34.2
|
1.0
|
HB2
|
B:ASP564
|
4.8
|
39.6
|
1.0
|
ND2
|
B:ASN606
|
4.9
|
36.9
|
1.0
|
HG23
|
B:THR604
|
4.9
|
37.8
|
1.0
|
HG22
|
B:THR502
|
5.0
|
35.3
|
1.0
|
|
Magnesium binding site 3 out
of 5 in 7uiy
Go back to
Magnesium Binding Sites List in 7uiy
Magnesium binding site 3 out
of 5 in the Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg804
b:49.7
occ:1.00
|
OG1
|
B:THR221
|
2.0
|
55.7
|
1.0
|
O1B
|
B:AGS801
|
2.0
|
52.9
|
1.0
|
O2B
|
B:AGS801
|
2.4
|
52.9
|
1.0
|
PB
|
B:AGS801
|
2.6
|
52.9
|
1.0
|
HB
|
B:THR221
|
2.6
|
55.7
|
1.0
|
HG21
|
B:THR221
|
2.7
|
55.7
|
1.0
|
CB
|
B:THR221
|
2.7
|
55.7
|
1.0
|
HH22
|
C:ARG340
|
3.1
|
42.2
|
1.0
|
CG2
|
B:THR221
|
3.2
|
55.7
|
1.0
|
NH2
|
C:ARG340
|
3.7
|
42.2
|
1.0
|
HG22
|
B:THR221
|
3.7
|
55.7
|
1.0
|
O5'
|
B:AGS801
|
3.7
|
52.9
|
1.0
|
O3A
|
B:AGS801
|
3.7
|
52.9
|
1.0
|
HH21
|
C:ARG340
|
3.8
|
42.2
|
1.0
|
OD1
|
B:ASP285
|
3.8
|
61.4
|
1.0
|
O3B
|
B:AGS801
|
3.9
|
52.9
|
1.0
|
HG23
|
B:THR221
|
3.9
|
55.7
|
1.0
|
H
|
B:THR221
|
4.1
|
55.7
|
1.0
|
CA
|
B:THR221
|
4.1
|
55.7
|
1.0
|
OD2
|
B:ASP285
|
4.2
|
61.4
|
1.0
|
O2A
|
B:AGS801
|
4.2
|
52.9
|
1.0
|
PA
|
B:AGS801
|
4.2
|
52.9
|
1.0
|
CG
|
B:ASP285
|
4.3
|
61.4
|
1.0
|
O3G
|
B:AGS801
|
4.4
|
52.9
|
1.0
|
HA
|
B:THR221
|
4.5
|
55.7
|
1.0
|
PG
|
B:AGS801
|
4.5
|
52.9
|
1.0
|
N
|
B:THR221
|
4.5
|
55.7
|
1.0
|
S1G
|
B:AGS801
|
4.5
|
52.9
|
1.0
|
H5'1
|
B:AGS801
|
4.6
|
52.9
|
1.0
|
HG3
|
B:LYS220
|
4.7
|
57.2
|
1.0
|
C5'
|
B:AGS801
|
4.7
|
52.9
|
1.0
|
HH12
|
C:ARG340
|
4.8
|
42.2
|
1.0
|
CZ
|
C:ARG340
|
4.8
|
42.2
|
1.0
|
HH21
|
C:ARG339
|
4.9
|
43.6
|
1.0
|
H5'2
|
B:AGS801
|
4.9
|
52.9
|
1.0
|
|
Magnesium binding site 4 out
of 5 in 7uiy
Go back to
Magnesium Binding Sites List in 7uiy
Magnesium binding site 4 out
of 5 in the Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg803
b:39.5
occ:1.00
|
HG23
|
C:THR502
|
1.9
|
30.2
|
1.0
|
HG21
|
C:THR502
|
2.0
|
30.2
|
1.0
|
CG2
|
C:THR502
|
2.3
|
30.2
|
1.0
|
S1G
|
C:AGS802
|
2.4
|
28.7
|
1.0
|
HG22
|
C:THR502
|
2.9
|
30.2
|
1.0
|
O3B
|
C:AGS802
|
3.0
|
28.7
|
1.0
|
PG
|
C:AGS802
|
3.1
|
28.7
|
1.0
|
HG1
|
C:THR502
|
3.2
|
30.2
|
1.0
|
O2B
|
C:AGS802
|
3.3
|
28.7
|
1.0
|
HH22
|
D:ARG643
|
3.3
|
34.9
|
1.0
|
O2A
|
C:AGS802
|
3.5
|
28.7
|
1.0
|
O3G
|
C:AGS802
|
3.5
|
28.7
|
1.0
|
CB
|
C:THR502
|
3.5
|
30.2
|
1.0
|
OG1
|
C:THR502
|
3.6
|
30.2
|
1.0
|
PB
|
C:AGS802
|
3.7
|
28.7
|
1.0
|
HH22
|
C:ARG702
|
3.8
|
35.7
|
1.0
|
OD1
|
C:ASP564
|
4.0
|
34.6
|
1.0
|
NH2
|
D:ARG643
|
4.0
|
34.9
|
1.0
|
H
|
C:THR502
|
4.0
|
30.2
|
1.0
|
HB
|
C:THR502
|
4.0
|
30.2
|
1.0
|
HH21
|
D:ARG643
|
4.1
|
34.9
|
1.0
|
HG1
|
C:THR604
|
4.2
|
31.5
|
1.0
|
O3A
|
C:AGS802
|
4.4
|
28.7
|
1.0
|
PA
|
C:AGS802
|
4.4
|
28.7
|
1.0
|
HB2
|
C:LYS501
|
4.5
|
32.5
|
1.0
|
HE3
|
C:LYS501
|
4.5
|
32.5
|
1.0
|
O2G
|
C:AGS802
|
4.5
|
28.7
|
1.0
|
N
|
C:THR502
|
4.5
|
30.2
|
1.0
|
NH2
|
C:ARG702
|
4.6
|
35.7
|
1.0
|
CA
|
C:THR502
|
4.7
|
30.2
|
1.0
|
OE1
|
C:GLU565
|
4.7
|
37.3
|
1.0
|
OD2
|
D:ASP582
|
4.7
|
36.5
|
1.0
|
CG
|
C:ASP564
|
4.7
|
34.6
|
1.0
|
O1A
|
C:AGS802
|
4.8
|
28.7
|
1.0
|
HH21
|
C:ARG702
|
4.9
|
35.7
|
1.0
|
OG1
|
C:THR604
|
4.9
|
31.5
|
1.0
|
HH12
|
D:ARG643
|
5.0
|
34.9
|
1.0
|
|
Magnesium binding site 5 out
of 5 in 7uiy
Go back to
Magnesium Binding Sites List in 7uiy
Magnesium binding site 5 out
of 5 in the Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Clpap Complex Bound to Clps N-Terminal Extension, Class Iiia within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg803
b:48.3
occ:1.00
|
HG21
|
D:THR221
|
1.8
|
33.8
|
1.0
|
O3B
|
D:AGS801
|
2.1
|
33.0
|
1.0
|
O2B
|
D:AGS801
|
2.4
|
33.0
|
1.0
|
PB
|
D:AGS801
|
2.4
|
33.0
|
1.0
|
O3A
|
D:AGS801
|
2.4
|
33.0
|
1.0
|
CG2
|
D:THR221
|
2.7
|
33.8
|
1.0
|
HG22
|
D:THR221
|
2.9
|
33.8
|
1.0
|
PG
|
D:AGS801
|
3.1
|
33.0
|
1.0
|
HG23
|
D:THR221
|
3.1
|
33.8
|
1.0
|
S1G
|
D:AGS801
|
3.1
|
33.0
|
1.0
|
HH22
|
E:ARG339
|
3.1
|
33.2
|
1.0
|
HH22
|
E:ARG340
|
3.3
|
34.1
|
1.0
|
O3G
|
D:AGS801
|
3.7
|
33.0
|
1.0
|
PA
|
D:AGS801
|
3.8
|
33.0
|
1.0
|
OG1
|
D:THR221
|
3.8
|
33.8
|
1.0
|
HG1
|
D:THR221
|
3.8
|
33.8
|
1.0
|
H
|
D:THR221
|
3.8
|
33.8
|
1.0
|
NH2
|
E:ARG339
|
3.8
|
33.2
|
1.0
|
CB
|
D:THR221
|
3.9
|
33.8
|
1.0
|
O1B
|
D:AGS801
|
3.9
|
33.0
|
1.0
|
NH2
|
E:ARG340
|
4.0
|
34.1
|
1.0
|
O5'
|
D:AGS801
|
4.1
|
33.0
|
1.0
|
O2A
|
D:AGS801
|
4.1
|
33.0
|
1.0
|
HH12
|
E:ARG340
|
4.1
|
34.1
|
1.0
|
HH21
|
E:ARG339
|
4.1
|
33.2
|
1.0
|
OD2
|
D:ASP285
|
4.3
|
38.0
|
1.0
|
O2G
|
D:AGS801
|
4.3
|
33.0
|
1.0
|
HH21
|
E:ARG340
|
4.5
|
34.1
|
1.0
|
HB
|
D:THR221
|
4.5
|
33.8
|
1.0
|
HH12
|
E:ARG339
|
4.5
|
33.2
|
1.0
|
N
|
D:THR221
|
4.6
|
33.8
|
1.0
|
HB2
|
D:LYS220
|
4.6
|
31.8
|
1.0
|
HZ3
|
D:LYS220
|
4.7
|
31.8
|
1.0
|
NH1
|
E:ARG340
|
4.7
|
34.1
|
1.0
|
OD1
|
D:ASP285
|
4.8
|
38.0
|
1.0
|
CZ
|
E:ARG340
|
4.8
|
34.1
|
1.0
|
CA
|
D:THR221
|
4.9
|
33.8
|
1.0
|
CZ
|
E:ARG339
|
4.9
|
33.2
|
1.0
|
HE2
|
D:LYS220
|
4.9
|
31.8
|
1.0
|
O1A
|
D:AGS801
|
4.9
|
33.0
|
1.0
|
CG
|
D:ASP285
|
5.0
|
38.0
|
1.0
|
|
Reference:
S.Kim,
X.Fei,
R.T.Sauer,
T.A.Baker.
Aaa+ Protease-Adaptor Structures Reveal Altered Conformations and Ring Specialization. Nat.Struct.Mol.Biol. V. 29 1068 2022.
ISSN: ESSN 1545-9985
PubMed: 36329286
DOI: 10.1038/S41594-022-00850-3
Page generated: Thu Oct 3 10:01:54 2024
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