Magnesium in PDB 7dy1: Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic
Enzymatic activity of Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic
All present enzymatic activity of Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic:
2.7.11.1;
Protein crystallography data
The structure of Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic, PDB code: 7dy1
was solved by
Y.Furuike,
S.Akiyama,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.28 /
2.20
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
131.103,
136.492,
190.772,
90,
90,
90
|
R / Rfree (%)
|
23.3 /
28.4
|
Magnesium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Magnesium atom in the Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic
(pdb code 7dy1). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 12 binding sites of Magnesium where determined in the
Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic, PDB code: 7dy1:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Magnesium binding site 1 out
of 12 in 7dy1
Go back to
Magnesium Binding Sites List in 7dy1
Magnesium binding site 1 out
of 12 in the Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg603
b:35.3
occ:1.00
|
OG1
|
A:THR54
|
2.0
|
17.1
|
1.0
|
O
|
A:HOH716
|
2.1
|
15.7
|
1.0
|
O2G
|
A:ATP601
|
2.1
|
17.3
|
1.0
|
O
|
A:HOH746
|
2.1
|
21.3
|
1.0
|
O2B
|
A:ATP601
|
2.2
|
18.5
|
1.0
|
CB
|
A:THR54
|
3.1
|
16.3
|
1.0
|
PG
|
A:ATP601
|
3.3
|
21.8
|
1.0
|
PB
|
A:ATP601
|
3.4
|
17.9
|
1.0
|
O3B
|
A:ATP601
|
3.6
|
18.1
|
1.0
|
O
|
A:HOH715
|
3.8
|
30.4
|
1.0
|
OD2
|
A:ASP146
|
3.8
|
29.6
|
1.0
|
O1G
|
A:ATP601
|
3.9
|
19.4
|
1.0
|
N
|
A:THR54
|
4.0
|
15.7
|
1.0
|
CG2
|
A:THR54
|
4.0
|
15.7
|
1.0
|
CA
|
A:THR54
|
4.1
|
16.8
|
1.0
|
OD1
|
A:ASP146
|
4.1
|
30.2
|
1.0
|
O1A
|
A:ATP601
|
4.1
|
22.4
|
1.0
|
O3A
|
A:ATP601
|
4.2
|
21.8
|
1.0
|
OE2
|
A:GLU79
|
4.2
|
45.9
|
1.0
|
NH2
|
B:ARG227
|
4.4
|
23.1
|
1.0
|
CG
|
A:ASP146
|
4.4
|
30.4
|
1.0
|
NE
|
B:ARG227
|
4.4
|
24.4
|
1.0
|
PA
|
A:ATP601
|
4.5
|
22.3
|
1.0
|
O1B
|
A:ATP601
|
4.6
|
17.5
|
1.0
|
O3G
|
A:ATP601
|
4.6
|
16.4
|
1.0
|
O2A
|
A:ATP601
|
4.6
|
19.8
|
1.0
|
CZ
|
B:ARG227
|
4.8
|
24.8
|
1.0
|
O
|
A:HOH712
|
4.9
|
44.2
|
1.0
|
|
Magnesium binding site 2 out
of 12 in 7dy1
Go back to
Magnesium Binding Sites List in 7dy1
Magnesium binding site 2 out
of 12 in the Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg604
b:19.1
occ:1.00
|
O
|
A:HOH719
|
1.8
|
15.4
|
1.0
|
O
|
A:HOH779
|
2.1
|
17.4
|
1.0
|
O2B
|
A:ATP602
|
2.1
|
16.2
|
1.0
|
O1G
|
A:ATP602
|
2.1
|
23.6
|
1.0
|
OG1
|
A:THR295
|
2.1
|
19.6
|
1.0
|
O
|
A:HOH722
|
2.2
|
19.2
|
1.0
|
CB
|
A:THR295
|
3.2
|
21.0
|
1.0
|
PB
|
A:ATP602
|
3.3
|
17.7
|
1.0
|
PG
|
A:ATP602
|
3.3
|
25.2
|
1.0
|
O3B
|
A:ATP602
|
3.4
|
21.9
|
1.0
|
O
|
A:HOH714
|
3.7
|
27.4
|
1.0
|
N
|
A:THR295
|
3.9
|
20.5
|
1.0
|
OE2
|
A:GLU319
|
3.9
|
32.1
|
1.0
|
O1A
|
A:ATP602
|
4.0
|
19.3
|
1.0
|
O3G
|
A:ATP602
|
4.0
|
26.1
|
1.0
|
OD1
|
A:ASP378
|
4.1
|
32.3
|
1.0
|
CA
|
A:THR295
|
4.1
|
22.6
|
1.0
|
OD2
|
A:ASP378
|
4.1
|
29.9
|
1.0
|
OE1
|
A:GLU318
|
4.2
|
39.2
|
1.0
|
O3A
|
A:ATP602
|
4.3
|
18.5
|
1.0
|
O
|
A:HOH764
|
4.3
|
19.6
|
1.0
|
CG2
|
A:THR295
|
4.3
|
20.5
|
1.0
|
O1B
|
A:ATP602
|
4.4
|
17.9
|
1.0
|
PA
|
A:ATP602
|
4.4
|
21.4
|
1.0
|
O2G
|
A:ATP602
|
4.5
|
27.5
|
1.0
|
O2A
|
A:ATP602
|
4.5
|
19.0
|
1.0
|
CG
|
A:ASP378
|
4.5
|
28.9
|
1.0
|
CB
|
A:LYS294
|
4.7
|
26.0
|
1.0
|
NH2
|
B:ARG459
|
4.7
|
21.7
|
1.0
|
C
|
A:LYS294
|
5.0
|
22.2
|
1.0
|
|
Magnesium binding site 3 out
of 12 in 7dy1
Go back to
Magnesium Binding Sites List in 7dy1
Magnesium binding site 3 out
of 12 in the Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg603
b:30.9
occ:1.00
|
O2G
|
B:ATP601
|
2.1
|
29.1
|
1.0
|
O
|
B:HOH764
|
2.1
|
21.8
|
1.0
|
OG1
|
B:THR54
|
2.1
|
19.5
|
1.0
|
O2B
|
B:ATP601
|
2.2
|
23.1
|
1.0
|
O
|
B:HOH728
|
2.3
|
24.7
|
1.0
|
O
|
B:HOH720
|
2.3
|
30.1
|
1.0
|
PG
|
B:ATP601
|
3.2
|
28.1
|
1.0
|
CB
|
B:THR54
|
3.3
|
20.4
|
1.0
|
PB
|
B:ATP601
|
3.4
|
21.9
|
1.0
|
O1G
|
B:ATP601
|
3.6
|
26.1
|
1.0
|
O3B
|
B:ATP601
|
3.6
|
24.3
|
1.0
|
NH2
|
C:ARG227
|
3.9
|
23.8
|
1.0
|
OD1
|
B:ASP146
|
4.0
|
33.5
|
1.0
|
O
|
B:HOH739
|
4.0
|
27.6
|
1.0
|
O3A
|
B:ATP601
|
4.1
|
23.6
|
1.0
|
O1A
|
B:ATP601
|
4.2
|
21.0
|
1.0
|
N
|
B:THR54
|
4.2
|
20.7
|
1.0
|
CG2
|
B:THR54
|
4.2
|
21.8
|
1.0
|
NE
|
C:ARG227
|
4.2
|
23.4
|
1.0
|
OE2
|
B:GLU79
|
4.3
|
40.6
|
1.0
|
CA
|
B:THR54
|
4.3
|
20.9
|
1.0
|
OD2
|
B:ASP146
|
4.4
|
35.5
|
1.0
|
CZ
|
C:ARG227
|
4.5
|
25.2
|
1.0
|
PA
|
B:ATP601
|
4.5
|
21.3
|
1.0
|
O3G
|
B:ATP601
|
4.5
|
28.8
|
1.0
|
O1B
|
B:ATP601
|
4.5
|
22.2
|
1.0
|
CG
|
B:ASP146
|
4.6
|
32.5
|
1.0
|
O2A
|
B:ATP601
|
4.7
|
18.0
|
1.0
|
|
Magnesium binding site 4 out
of 12 in 7dy1
Go back to
Magnesium Binding Sites List in 7dy1
Magnesium binding site 4 out
of 12 in the Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg604
b:23.8
occ:1.00
|
O2B
|
B:ATP602
|
1.9
|
21.0
|
1.0
|
OG1
|
B:THR295
|
2.0
|
21.8
|
1.0
|
O
|
B:HOH740
|
2.0
|
20.2
|
1.0
|
O
|
B:HOH745
|
2.0
|
27.2
|
1.0
|
O2G
|
B:ATP602
|
2.1
|
25.4
|
1.0
|
O
|
B:HOH753
|
2.2
|
22.8
|
1.0
|
PB
|
B:ATP602
|
3.1
|
23.9
|
1.0
|
PG
|
B:ATP602
|
3.3
|
26.8
|
1.0
|
CB
|
B:THR295
|
3.3
|
24.9
|
1.0
|
O3B
|
B:ATP602
|
3.4
|
24.0
|
1.0
|
N
|
B:THR295
|
3.9
|
22.3
|
1.0
|
O
|
B:HOH729
|
3.9
|
29.7
|
1.0
|
OE1
|
B:GLU318
|
4.0
|
40.9
|
1.0
|
OD1
|
B:ASP378
|
4.0
|
22.7
|
1.0
|
O
|
B:HOH771
|
4.1
|
26.6
|
1.0
|
O3G
|
B:ATP602
|
4.1
|
25.4
|
1.0
|
CA
|
B:THR295
|
4.1
|
23.8
|
1.0
|
O3A
|
B:ATP602
|
4.1
|
22.2
|
1.0
|
O1A
|
B:ATP602
|
4.2
|
22.4
|
1.0
|
O1B
|
B:ATP602
|
4.2
|
22.3
|
1.0
|
OD2
|
B:ASP378
|
4.2
|
23.1
|
1.0
|
OE2
|
B:GLU319
|
4.2
|
28.3
|
1.0
|
CG2
|
B:THR295
|
4.3
|
24.2
|
1.0
|
O1G
|
B:ATP602
|
4.4
|
29.0
|
1.0
|
PA
|
B:ATP602
|
4.5
|
22.6
|
1.0
|
CG
|
B:ASP378
|
4.5
|
23.5
|
1.0
|
O2A
|
B:ATP602
|
4.6
|
20.1
|
1.0
|
NH2
|
C:ARG459
|
4.7
|
26.8
|
1.0
|
CB
|
B:LYS294
|
4.7
|
26.7
|
1.0
|
C
|
B:LYS294
|
4.9
|
22.1
|
1.0
|
|
Magnesium binding site 5 out
of 12 in 7dy1
Go back to
Magnesium Binding Sites List in 7dy1
Magnesium binding site 5 out
of 12 in the Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg603
b:30.4
occ:1.00
|
O2G
|
C:ATP601
|
2.0
|
24.9
|
1.0
|
O2B
|
C:ATP601
|
2.1
|
22.5
|
1.0
|
O
|
C:HOH734
|
2.1
|
22.5
|
1.0
|
O
|
C:HOH719
|
2.2
|
31.0
|
1.0
|
O
|
C:HOH809
|
2.2
|
30.3
|
1.0
|
OG1
|
C:THR54
|
2.2
|
18.0
|
1.0
|
PG
|
C:ATP601
|
3.2
|
25.9
|
1.0
|
PB
|
C:ATP601
|
3.2
|
22.8
|
1.0
|
CB
|
C:THR54
|
3.3
|
17.6
|
1.0
|
O3B
|
C:ATP601
|
3.5
|
22.2
|
1.0
|
O1G
|
C:ATP601
|
3.9
|
26.9
|
1.0
|
O3A
|
C:ATP601
|
4.0
|
20.1
|
1.0
|
O1A
|
C:ATP601
|
4.1
|
20.4
|
1.0
|
OE2
|
C:GLU79
|
4.1
|
31.8
|
1.0
|
OD2
|
C:ASP146
|
4.1
|
30.4
|
1.0
|
NH2
|
D:ARG227
|
4.1
|
24.5
|
1.0
|
NE
|
D:ARG227
|
4.1
|
26.0
|
1.0
|
N
|
C:THR54
|
4.1
|
18.8
|
1.0
|
CG2
|
C:THR54
|
4.2
|
17.4
|
1.0
|
OD1
|
C:ASP146
|
4.2
|
28.9
|
1.0
|
CA
|
C:THR54
|
4.3
|
17.5
|
1.0
|
O
|
C:HOH829
|
4.3
|
31.4
|
1.0
|
O
|
C:HOH781
|
4.4
|
30.8
|
1.0
|
O3G
|
C:ATP601
|
4.4
|
28.5
|
1.0
|
CZ
|
D:ARG227
|
4.5
|
25.2
|
1.0
|
O1B
|
C:ATP601
|
4.5
|
21.0
|
1.0
|
PA
|
C:ATP601
|
4.5
|
20.8
|
1.0
|
CG
|
C:ASP146
|
4.6
|
29.2
|
1.0
|
O2A
|
C:ATP601
|
4.7
|
18.9
|
1.0
|
O
|
C:HOH738
|
4.8
|
22.3
|
1.0
|
|
Magnesium binding site 6 out
of 12 in 7dy1
Go back to
Magnesium Binding Sites List in 7dy1
Magnesium binding site 6 out
of 12 in the Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg604
b:25.6
occ:1.00
|
O1B
|
C:ATP602
|
2.0
|
17.8
|
1.0
|
O
|
C:HOH732
|
2.0
|
20.6
|
1.0
|
OG1
|
C:THR295
|
2.1
|
21.2
|
1.0
|
O
|
C:HOH722
|
2.3
|
29.5
|
1.0
|
O2G
|
C:ATP602
|
2.3
|
32.6
|
1.0
|
O
|
C:HOH701
|
2.3
|
15.4
|
1.0
|
CB
|
C:THR295
|
3.2
|
22.7
|
1.0
|
PG
|
C:ATP602
|
3.2
|
29.3
|
1.0
|
PB
|
C:ATP602
|
3.2
|
21.2
|
1.0
|
O3B
|
C:ATP602
|
3.5
|
23.8
|
1.0
|
O3G
|
C:ATP602
|
3.5
|
37.7
|
1.0
|
OE1
|
C:GLU319
|
3.8
|
27.8
|
1.0
|
OE2
|
C:GLU318
|
3.9
|
41.9
|
1.0
|
N
|
C:THR295
|
4.0
|
21.9
|
1.0
|
O1A
|
C:ATP602
|
4.0
|
21.8
|
1.0
|
OD1
|
C:ASP378
|
4.1
|
27.8
|
1.0
|
OD2
|
C:ASP378
|
4.1
|
25.3
|
1.0
|
O
|
C:HOH727
|
4.1
|
23.9
|
1.0
|
CA
|
C:THR295
|
4.1
|
22.0
|
1.0
|
O3A
|
C:ATP602
|
4.2
|
21.8
|
1.0
|
CG2
|
C:THR295
|
4.2
|
22.6
|
1.0
|
O2B
|
C:ATP602
|
4.3
|
20.1
|
1.0
|
NH2
|
D:ARG459
|
4.4
|
20.4
|
1.0
|
CG
|
C:ASP378
|
4.5
|
26.1
|
1.0
|
PA
|
C:ATP602
|
4.5
|
22.6
|
1.0
|
O1G
|
C:ATP602
|
4.6
|
33.2
|
1.0
|
O2A
|
C:ATP602
|
4.7
|
20.8
|
1.0
|
CD
|
C:GLU319
|
5.0
|
31.0
|
1.0
|
CB
|
C:LYS294
|
5.0
|
24.3
|
1.0
|
|
Magnesium binding site 7 out
of 12 in 7dy1
Go back to
Magnesium Binding Sites List in 7dy1
Magnesium binding site 7 out
of 12 in the Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg603
b:17.6
occ:1.00
|
O
|
D:HOH717
|
1.9
|
20.4
|
1.0
|
O2B
|
D:ATP601
|
2.0
|
16.0
|
1.0
|
OG1
|
D:THR54
|
2.0
|
15.9
|
1.0
|
O
|
D:HOH778
|
2.1
|
20.6
|
1.0
|
O2G
|
D:ATP601
|
2.1
|
20.4
|
1.0
|
O
|
D:HOH806
|
2.2
|
16.3
|
1.0
|
CB
|
D:THR54
|
3.0
|
16.2
|
1.0
|
PB
|
D:ATP601
|
3.1
|
18.8
|
1.0
|
PG
|
D:ATP601
|
3.3
|
21.1
|
1.0
|
O3B
|
D:ATP601
|
3.4
|
19.4
|
1.0
|
O1A
|
D:ATP601
|
3.9
|
22.2
|
1.0
|
O1G
|
D:ATP601
|
3.9
|
20.9
|
1.0
|
O3A
|
D:ATP601
|
4.0
|
20.5
|
1.0
|
OD2
|
D:ASP146
|
4.0
|
27.6
|
1.0
|
NH2
|
E:ARG227
|
4.0
|
20.0
|
1.0
|
CG2
|
D:THR54
|
4.0
|
17.1
|
1.0
|
N
|
D:THR54
|
4.0
|
14.9
|
1.0
|
CA
|
D:THR54
|
4.1
|
17.1
|
1.0
|
NE
|
E:ARG227
|
4.2
|
19.2
|
1.0
|
O
|
E:HOH820
|
4.3
|
18.9
|
1.0
|
PA
|
D:ATP601
|
4.3
|
21.7
|
1.0
|
O1B
|
D:ATP601
|
4.4
|
16.5
|
1.0
|
O
|
D:HOH741
|
4.4
|
22.7
|
1.0
|
OD1
|
D:ASP146
|
4.4
|
28.7
|
1.0
|
CZ
|
E:ARG227
|
4.5
|
18.7
|
1.0
|
OE2
|
D:GLU79
|
4.5
|
44.2
|
1.0
|
O3G
|
D:ATP601
|
4.5
|
23.0
|
1.0
|
O2A
|
D:ATP601
|
4.5
|
17.8
|
1.0
|
CG
|
D:ASP146
|
4.6
|
27.9
|
1.0
|
|
Magnesium binding site 8 out
of 12 in 7dy1
Go back to
Magnesium Binding Sites List in 7dy1
Magnesium binding site 8 out
of 12 in the Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg604
b:17.3
occ:1.00
|
OG1
|
D:THR295
|
2.0
|
18.7
|
1.0
|
O
|
D:HOH754
|
2.0
|
19.4
|
1.0
|
O
|
D:HOH819
|
2.0
|
18.8
|
1.0
|
O
|
D:HOH750
|
2.1
|
20.5
|
1.0
|
O1B
|
D:ATP602
|
2.2
|
18.1
|
1.0
|
O3G
|
D:ATP602
|
2.2
|
25.5
|
1.0
|
CB
|
D:THR295
|
3.3
|
21.3
|
1.0
|
PB
|
D:ATP602
|
3.4
|
19.6
|
1.0
|
PG
|
D:ATP602
|
3.4
|
27.0
|
1.0
|
O3B
|
D:ATP602
|
3.4
|
22.1
|
1.0
|
O
|
D:HOH723
|
4.0
|
22.5
|
1.0
|
OD2
|
D:ASP378
|
4.1
|
23.4
|
1.0
|
N
|
D:THR295
|
4.1
|
19.0
|
1.0
|
O1A
|
D:ATP602
|
4.1
|
20.2
|
1.0
|
OD1
|
D:ASP378
|
4.2
|
26.1
|
1.0
|
OE1
|
D:GLU318
|
4.2
|
40.3
|
1.0
|
CA
|
D:THR295
|
4.2
|
21.5
|
1.0
|
O
|
D:HOH795
|
4.2
|
25.2
|
1.0
|
CG2
|
D:THR295
|
4.2
|
19.6
|
1.0
|
O3A
|
D:ATP602
|
4.3
|
20.3
|
1.0
|
OE2
|
D:GLU319
|
4.3
|
30.9
|
1.0
|
O2G
|
D:ATP602
|
4.3
|
25.1
|
1.0
|
O1G
|
D:ATP602
|
4.4
|
23.9
|
1.0
|
O2B
|
D:ATP602
|
4.5
|
16.5
|
1.0
|
CG
|
D:ASP378
|
4.5
|
23.2
|
1.0
|
NH2
|
E:ARG459
|
4.6
|
20.7
|
1.0
|
PA
|
D:ATP602
|
4.6
|
19.6
|
1.0
|
O2A
|
D:ATP602
|
4.8
|
20.9
|
1.0
|
|
Magnesium binding site 9 out
of 12 in 7dy1
Go back to
Magnesium Binding Sites List in 7dy1
Magnesium binding site 9 out
of 12 in the Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 9 of Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg603
b:25.3
occ:1.00
|
OG1
|
E:THR54
|
1.9
|
20.7
|
1.0
|
O
|
E:HOH731
|
2.0
|
24.6
|
1.0
|
O
|
E:HOH721
|
2.0
|
35.6
|
1.0
|
O
|
E:HOH795
|
2.1
|
34.1
|
1.0
|
O2B
|
E:ATP601
|
2.2
|
17.3
|
1.0
|
O2G
|
E:ATP601
|
2.2
|
28.6
|
1.0
|
CB
|
E:THR54
|
3.2
|
22.9
|
1.0
|
PG
|
E:ATP601
|
3.5
|
26.3
|
1.0
|
PB
|
E:ATP601
|
3.5
|
21.2
|
1.0
|
OD1
|
E:ASP146
|
3.8
|
36.0
|
1.0
|
O3B
|
E:ATP601
|
3.9
|
22.9
|
1.0
|
OD2
|
E:ASP146
|
3.9
|
32.5
|
1.0
|
N
|
E:THR54
|
4.0
|
22.0
|
1.0
|
O1G
|
E:ATP601
|
4.0
|
25.5
|
1.0
|
CA
|
E:THR54
|
4.1
|
22.2
|
1.0
|
CG2
|
E:THR54
|
4.1
|
24.4
|
1.0
|
O
|
F:HOH824
|
4.1
|
40.7
|
1.0
|
CG
|
E:ASP146
|
4.3
|
32.8
|
1.0
|
O3A
|
E:ATP601
|
4.3
|
21.2
|
1.0
|
NH2
|
F:ARG227
|
4.4
|
21.7
|
1.0
|
O1A
|
E:ATP601
|
4.4
|
21.3
|
1.0
|
NE
|
F:ARG227
|
4.5
|
22.3
|
1.0
|
O1B
|
E:ATP601
|
4.6
|
24.1
|
1.0
|
PA
|
E:ATP601
|
4.7
|
20.0
|
1.0
|
O3G
|
E:ATP601
|
4.7
|
28.1
|
1.0
|
O2A
|
E:ATP601
|
4.8
|
19.4
|
1.0
|
O
|
E:HOH759
|
4.8
|
42.2
|
1.0
|
CZ
|
F:ARG227
|
4.9
|
22.6
|
1.0
|
CB
|
E:LYS53
|
5.0
|
18.2
|
1.0
|
|
Magnesium binding site 10 out
of 12 in 7dy1
Go back to
Magnesium Binding Sites List in 7dy1
Magnesium binding site 10 out
of 12 in the Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 10 of Crystal Structure of Cyanobacterial Circadian Clock Protein Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg604
b:27.0
occ:1.00
|
O1B
|
E:ATP602
|
2.0
|
17.0
|
1.0
|
O
|
E:HOH767
|
2.0
|
23.8
|
1.0
|
O
|
E:HOH740
|
2.0
|
24.6
|
1.0
|
O1G
|
E:ATP602
|
2.1
|
24.6
|
1.0
|
OG1
|
E:THR295
|
2.1
|
19.6
|
1.0
|
O
|
E:HOH739
|
2.3
|
17.3
|
1.0
|
PB
|
E:ATP602
|
3.2
|
20.5
|
1.0
|
CB
|
E:THR295
|
3.2
|
20.7
|
1.0
|
PG
|
E:ATP602
|
3.3
|
26.8
|
1.0
|
O3B
|
E:ATP602
|
3.4
|
23.3
|
1.0
|
OE2
|
E:GLU319
|
4.0
|
34.7
|
1.0
|
N
|
E:THR295
|
4.0
|
20.3
|
1.0
|
OD2
|
E:ASP378
|
4.0
|
27.8
|
1.0
|
OE1
|
E:GLU318
|
4.0
|
50.5
|
1.0
|
OD1
|
E:ASP378
|
4.1
|
27.9
|
1.0
|
CA
|
E:THR295
|
4.1
|
21.4
|
1.0
|
O3A
|
E:ATP602
|
4.2
|
22.1
|
1.0
|
O1A
|
E:ATP602
|
4.2
|
22.1
|
1.0
|
O3G
|
E:ATP602
|
4.2
|
25.6
|
1.0
|
O
|
E:HOH702
|
4.2
|
39.9
|
1.0
|
CG2
|
E:THR295
|
4.2
|
21.7
|
1.0
|
CG
|
E:LYS294
|
4.3
|
26.2
|
1.0
|
O2B
|
E:ATP602
|
4.3
|
19.8
|
1.0
|
O
|
E:HOH763
|
4.4
|
20.2
|
1.0
|
O2G
|
E:ATP602
|
4.4
|
26.1
|
1.0
|
CG
|
E:ASP378
|
4.5
|
26.7
|
1.0
|
PA
|
E:ATP602
|
4.6
|
21.5
|
1.0
|
O2A
|
E:ATP602
|
4.7
|
23.7
|
1.0
|
NH2
|
F:ARG459
|
4.7
|
29.0
|
1.0
|
CD
|
E:GLU318
|
5.0
|
45.1
|
1.0
|
|
Reference:
Y.Furuike,
A.Mukaiyama,
S.I.Koda,
D.Simon,
D.Ouyang,
K.Ito-Miwa,
S.Saito,
E.Yamashita,
T.Nishiwaki-Ohkawa,
K.Terauchi,
T.Kondo,
S.Akiyama.
Regulation Mechanisms of the Dual Atpase in Kaic. Proc.Natl.Acad.Sci.Usa V. 119 27119 2022.
ISSN: ESSN 1091-6490
PubMed: 35507871
DOI: 10.1073/PNAS.2119627119
Page generated: Wed Oct 2 17:32:39 2024
|