Magnesium in PDB 4tl7: Crystal Structure of N-Terminal C1 Domain of Kaic
Enzymatic activity of Crystal Structure of N-Terminal C1 Domain of Kaic
All present enzymatic activity of Crystal Structure of N-Terminal C1 Domain of Kaic:
2.7.11.1;
Protein crystallography data
The structure of Crystal Structure of N-Terminal C1 Domain of Kaic, PDB code: 4tl7
was solved by
J.Abe,
T.B.Hiyama,
A.Mukaiyama,
S.Son,
S.Akiyama,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
45.85 /
1.94
|
Space group
|
P 31 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
108.165,
108.165,
224.880,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
15 /
19.1
|
Other elements in 4tl7:
The structure of Crystal Structure of N-Terminal C1 Domain of Kaic also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of N-Terminal C1 Domain of Kaic
(pdb code 4tl7). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 6 binding sites of Magnesium where determined in the
Crystal Structure of N-Terminal C1 Domain of Kaic, PDB code: 4tl7:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
Magnesium binding site 1 out
of 6 in 4tl7
Go back to
Magnesium Binding Sites List in 4tl7
Magnesium binding site 1 out
of 6 in the Crystal Structure of N-Terminal C1 Domain of 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 N-Terminal C1 Domain of Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg302
b:19.9
occ:1.00
|
O1G
|
A:ATP301
|
2.0
|
19.6
|
1.0
|
O1B
|
A:ATP301
|
2.1
|
17.3
|
1.0
|
O
|
A:HOH498
|
2.1
|
19.6
|
1.0
|
OG1
|
A:THR53
|
2.1
|
20.7
|
1.0
|
O
|
A:HOH499
|
2.1
|
20.5
|
1.0
|
O
|
A:HOH497
|
2.1
|
21.1
|
1.0
|
PB
|
A:ATP301
|
3.2
|
19.3
|
1.0
|
CB
|
A:THR53
|
3.2
|
23.4
|
1.0
|
PG
|
A:ATP301
|
3.3
|
23.5
|
1.0
|
O3B
|
A:ATP301
|
3.3
|
30.1
|
1.0
|
O3G
|
A:ATP301
|
3.9
|
29.4
|
1.0
|
OD2
|
A:ASP145
|
3.9
|
23.0
|
0.6
|
N
|
A:THR53
|
4.0
|
18.0
|
1.0
|
O
|
A:HOH432
|
4.0
|
23.9
|
1.0
|
O1A
|
A:ATP301
|
4.1
|
23.0
|
1.0
|
OD2
|
A:ASP145
|
4.1
|
22.5
|
0.4
|
CA
|
A:THR53
|
4.1
|
18.6
|
1.0
|
O
|
B:HOH479
|
4.2
|
44.7
|
1.0
|
O
|
A:HOH520
|
4.2
|
30.5
|
1.0
|
OD1
|
A:ASP145
|
4.2
|
23.3
|
0.6
|
OD1
|
A:ASP145
|
4.2
|
23.1
|
0.4
|
O3A
|
A:ATP301
|
4.2
|
20.0
|
1.0
|
CG2
|
A:THR53
|
4.3
|
19.9
|
1.0
|
O2B
|
A:ATP301
|
4.3
|
17.7
|
1.0
|
NH2
|
B:ARG226
|
4.4
|
20.0
|
1.0
|
NE
|
B:ARG226
|
4.5
|
22.4
|
1.0
|
O2G
|
A:ATP301
|
4.5
|
37.1
|
1.0
|
CG
|
A:ASP145
|
4.5
|
24.6
|
0.6
|
PA
|
A:ATP301
|
4.6
|
22.1
|
1.0
|
O
|
A:HOH459
|
4.6
|
35.9
|
1.0
|
CG
|
A:ASP145
|
4.6
|
24.8
|
0.4
|
O2A
|
A:ATP301
|
4.8
|
26.6
|
1.0
|
CZ
|
B:ARG226
|
4.8
|
24.0
|
1.0
|
CB
|
A:LYS52
|
5.0
|
16.9
|
1.0
|
|
Magnesium binding site 2 out
of 6 in 4tl7
Go back to
Magnesium Binding Sites List in 4tl7
Magnesium binding site 2 out
of 6 in the Crystal Structure of N-Terminal C1 Domain of 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 N-Terminal C1 Domain of Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg302
b:21.4
occ:1.00
|
O1B
|
B:ATP301
|
2.0
|
19.1
|
1.0
|
O1G
|
B:ATP301
|
2.0
|
21.6
|
1.0
|
O
|
B:HOH493
|
2.1
|
21.8
|
1.0
|
OG1
|
B:THR53
|
2.1
|
21.4
|
1.0
|
O
|
B:HOH494
|
2.1
|
24.6
|
1.0
|
O
|
B:HOH495
|
2.1
|
20.2
|
1.0
|
CB
|
B:THR53
|
3.1
|
26.4
|
1.0
|
PB
|
B:ATP301
|
3.2
|
19.7
|
1.0
|
PG
|
B:ATP301
|
3.3
|
24.7
|
1.0
|
O3B
|
B:ATP301
|
3.4
|
27.7
|
1.0
|
N
|
B:THR53
|
3.9
|
21.6
|
1.0
|
OD2
|
B:ASP145
|
4.0
|
24.9
|
0.7
|
O
|
B:HOH441
|
4.0
|
28.9
|
1.0
|
O3G
|
B:ATP301
|
4.0
|
27.7
|
1.0
|
OD2
|
B:ASP145
|
4.0
|
25.8
|
0.3
|
CA
|
B:THR53
|
4.1
|
20.9
|
1.0
|
OD1
|
B:ASP145
|
4.1
|
26.9
|
0.7
|
O2A
|
B:ATP301
|
4.1
|
26.3
|
1.0
|
OD1
|
B:ASP145
|
4.1
|
26.7
|
0.3
|
O
|
B:HOH433
|
4.2
|
27.5
|
1.0
|
O3A
|
B:ATP301
|
4.2
|
20.0
|
1.0
|
O2B
|
B:ATP301
|
4.3
|
20.8
|
1.0
|
CG2
|
B:THR53
|
4.3
|
21.1
|
1.0
|
O
|
B:HOH506
|
4.3
|
34.5
|
1.0
|
CG
|
B:ASP145
|
4.5
|
25.7
|
0.7
|
CG
|
B:ASP145
|
4.5
|
26.2
|
0.3
|
O2G
|
B:ATP301
|
4.5
|
40.6
|
1.0
|
NE
|
C:ARG226
|
4.6
|
23.8
|
1.0
|
NH2
|
C:ARG226
|
4.6
|
23.6
|
1.0
|
PA
|
B:ATP301
|
4.6
|
22.6
|
1.0
|
O1A
|
B:ATP301
|
4.8
|
28.1
|
1.0
|
C
|
B:LYS52
|
5.0
|
20.1
|
1.0
|
|
Magnesium binding site 3 out
of 6 in 4tl7
Go back to
Magnesium Binding Sites List in 4tl7
Magnesium binding site 3 out
of 6 in the Crystal Structure of N-Terminal C1 Domain of 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 N-Terminal C1 Domain of Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg302
b:22.7
occ:1.00
|
O2B
|
C:ATP301
|
2.0
|
16.5
|
1.0
|
O
|
C:HOH500
|
2.0
|
19.7
|
1.0
|
OG1
|
C:THR53
|
2.1
|
22.8
|
1.0
|
O2G
|
C:ATP301
|
2.1
|
23.9
|
1.0
|
O
|
C:HOH502
|
2.1
|
20.3
|
1.0
|
O
|
C:HOH501
|
2.2
|
22.7
|
1.0
|
CB
|
C:THR53
|
3.2
|
24.2
|
1.0
|
PB
|
C:ATP301
|
3.2
|
20.4
|
1.0
|
PG
|
C:ATP301
|
3.3
|
26.8
|
1.0
|
O3B
|
C:ATP301
|
3.4
|
31.8
|
1.0
|
O1G
|
C:ATP301
|
3.8
|
30.6
|
1.0
|
O
|
C:HOH521
|
3.9
|
27.3
|
1.0
|
OD2
|
C:ASP145
|
3.9
|
27.8
|
0.6
|
N
|
C:THR53
|
3.9
|
16.9
|
1.0
|
OD2
|
C:ASP145
|
4.0
|
24.7
|
0.5
|
CA
|
C:THR53
|
4.1
|
20.8
|
1.0
|
OD1
|
C:ASP145
|
4.1
|
24.9
|
0.6
|
O2A
|
C:ATP301
|
4.1
|
24.9
|
1.0
|
O
|
C:HOH520
|
4.2
|
35.5
|
1.0
|
O3A
|
C:ATP301
|
4.2
|
20.6
|
1.0
|
OD1
|
C:ASP145
|
4.2
|
25.7
|
0.5
|
CG2
|
C:THR53
|
4.3
|
22.3
|
1.0
|
O1B
|
C:ATP301
|
4.3
|
22.2
|
1.0
|
O
|
C:HOH441
|
4.4
|
33.6
|
1.0
|
CG
|
C:ASP145
|
4.4
|
28.0
|
0.6
|
NH2
|
D:ARG226
|
4.5
|
24.8
|
1.0
|
NE
|
D:ARG226
|
4.5
|
23.0
|
1.0
|
CG
|
C:ASP145
|
4.5
|
27.0
|
0.5
|
O3G
|
C:ATP301
|
4.6
|
35.1
|
1.0
|
PA
|
C:ATP301
|
4.6
|
22.7
|
1.0
|
CZ
|
D:ARG226
|
4.9
|
26.6
|
1.0
|
O1A
|
C:ATP301
|
4.9
|
25.0
|
1.0
|
CB
|
C:LYS52
|
4.9
|
24.1
|
1.0
|
|
Magnesium binding site 4 out
of 6 in 4tl7
Go back to
Magnesium Binding Sites List in 4tl7
Magnesium binding site 4 out
of 6 in the Crystal Structure of N-Terminal C1 Domain of 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 N-Terminal C1 Domain of Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg302
b:22.6
occ:1.00
|
O3G
|
D:ATP301
|
1.9
|
20.2
|
1.0
|
OG1
|
D:THR53
|
2.1
|
20.6
|
1.0
|
O2B
|
D:ATP301
|
2.1
|
18.3
|
1.0
|
O
|
D:HOH516
|
2.1
|
21.3
|
1.0
|
O
|
D:HOH515
|
2.1
|
20.7
|
1.0
|
O
|
D:HOH514
|
2.1
|
20.1
|
1.0
|
CB
|
D:THR53
|
3.1
|
19.0
|
1.0
|
PG
|
D:ATP301
|
3.2
|
25.7
|
1.0
|
PB
|
D:ATP301
|
3.2
|
17.0
|
1.0
|
O3B
|
D:ATP301
|
3.4
|
37.5
|
1.0
|
OD2
|
D:ASP145
|
3.9
|
22.8
|
0.6
|
N
|
D:THR53
|
3.9
|
19.0
|
1.0
|
O1G
|
D:ATP301
|
4.0
|
31.4
|
1.0
|
O
|
D:HOH536
|
4.0
|
53.6
|
1.0
|
O
|
D:HOH443
|
4.1
|
29.2
|
1.0
|
CA
|
D:THR53
|
4.1
|
20.4
|
1.0
|
OD2
|
D:ASP145
|
4.1
|
23.6
|
0.4
|
O2A
|
D:ATP301
|
4.1
|
21.1
|
1.0
|
O2G
|
D:ATP301
|
4.2
|
45.2
|
1.0
|
OD1
|
D:ASP145
|
4.2
|
24.7
|
0.4
|
O
|
D:HOH440
|
4.2
|
26.9
|
1.0
|
CG2
|
D:THR53
|
4.2
|
24.4
|
1.0
|
O3A
|
D:ATP301
|
4.2
|
19.4
|
1.0
|
OD1
|
D:ASP145
|
4.2
|
26.1
|
0.6
|
O1B
|
D:ATP301
|
4.3
|
17.4
|
1.0
|
NH2
|
E:ARG226
|
4.4
|
28.7
|
1.0
|
NE
|
E:ARG226
|
4.5
|
25.2
|
1.0
|
CG
|
D:ASP145
|
4.5
|
24.9
|
0.6
|
O
|
D:HOH450
|
4.5
|
32.3
|
1.0
|
PA
|
D:ATP301
|
4.6
|
23.1
|
1.0
|
CG
|
D:ASP145
|
4.6
|
24.5
|
0.4
|
O1A
|
D:ATP301
|
4.8
|
27.3
|
1.0
|
CZ
|
E:ARG226
|
4.9
|
28.4
|
1.0
|
CB
|
D:LYS52
|
5.0
|
19.1
|
1.0
|
|
Magnesium binding site 5 out
of 6 in 4tl7
Go back to
Magnesium Binding Sites List in 4tl7
Magnesium binding site 5 out
of 6 in the Crystal Structure of N-Terminal C1 Domain of 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 N-Terminal C1 Domain of Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg302
b:19.7
occ:1.00
|
O3G
|
E:ATP301
|
2.0
|
21.6
|
1.0
|
O
|
E:HOH502
|
2.0
|
21.7
|
1.0
|
O2B
|
E:ATP301
|
2.1
|
18.9
|
1.0
|
OG1
|
E:THR53
|
2.1
|
19.2
|
1.0
|
O
|
E:HOH503
|
2.1
|
20.1
|
1.0
|
O
|
E:HOH501
|
2.1
|
18.4
|
1.0
|
CB
|
E:THR53
|
3.2
|
18.3
|
1.0
|
PG
|
E:ATP301
|
3.2
|
24.1
|
1.0
|
PB
|
E:ATP301
|
3.2
|
20.0
|
1.0
|
O3B
|
E:ATP301
|
3.4
|
29.3
|
1.0
|
O2G
|
E:ATP301
|
3.8
|
26.0
|
1.0
|
O
|
E:HOH425
|
3.9
|
25.5
|
1.0
|
OD2
|
E:ASP145
|
3.9
|
23.7
|
0.6
|
N
|
E:THR53
|
4.0
|
22.9
|
1.0
|
OD2
|
E:ASP145
|
4.0
|
23.3
|
0.4
|
O1A
|
E:ATP301
|
4.0
|
22.6
|
1.0
|
CA
|
E:THR53
|
4.1
|
24.7
|
1.0
|
OD1
|
E:ASP145
|
4.2
|
22.7
|
0.6
|
O
|
E:HOH521
|
4.2
|
28.4
|
1.0
|
OD1
|
E:ASP145
|
4.2
|
23.6
|
0.4
|
O3A
|
E:ATP301
|
4.2
|
20.9
|
1.0
|
CG2
|
E:THR53
|
4.3
|
18.9
|
1.0
|
O1B
|
E:ATP301
|
4.3
|
20.4
|
1.0
|
NH2
|
F:ARG226
|
4.4
|
23.8
|
1.0
|
NE
|
F:ARG226
|
4.4
|
22.7
|
1.0
|
O1G
|
E:ATP301
|
4.4
|
36.0
|
1.0
|
O
|
E:HOH519
|
4.5
|
31.9
|
1.0
|
CG
|
E:ASP145
|
4.5
|
23.5
|
0.6
|
CG
|
E:ASP145
|
4.5
|
24.6
|
0.4
|
PA
|
E:ATP301
|
4.6
|
23.1
|
1.0
|
O2A
|
E:ATP301
|
4.8
|
28.6
|
1.0
|
CZ
|
F:ARG226
|
4.8
|
26.5
|
1.0
|
CB
|
E:LYS52
|
5.0
|
21.1
|
1.0
|
|
Magnesium binding site 6 out
of 6 in 4tl7
Go back to
Magnesium Binding Sites List in 4tl7
Magnesium binding site 6 out
of 6 in the Crystal Structure of N-Terminal C1 Domain of 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 N-Terminal C1 Domain of Kaic within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg302
b:24.1
occ:1.00
|
O
|
F:HOH486
|
2.0
|
21.0
|
1.0
|
O2B
|
F:ATP301
|
2.0
|
19.1
|
1.0
|
O2G
|
F:ATP301
|
2.0
|
23.0
|
1.0
|
OG1
|
F:THR53
|
2.1
|
26.3
|
1.0
|
O
|
F:HOH488
|
2.1
|
22.2
|
1.0
|
O
|
F:HOH487
|
2.2
|
27.2
|
1.0
|
PB
|
F:ATP301
|
3.1
|
21.1
|
1.0
|
CB
|
F:THR53
|
3.2
|
24.8
|
1.0
|
PG
|
F:ATP301
|
3.2
|
27.6
|
1.0
|
O3B
|
F:ATP301
|
3.3
|
29.0
|
1.0
|
N
|
F:THR53
|
3.8
|
20.4
|
1.0
|
O3G
|
F:ATP301
|
3.9
|
32.7
|
1.0
|
OD2
|
F:ASP145
|
4.0
|
27.0
|
0.6
|
O1A
|
F:ATP301
|
4.1
|
28.0
|
1.0
|
CA
|
F:THR53
|
4.1
|
22.7
|
1.0
|
O
|
F:HOH423
|
4.1
|
29.9
|
1.0
|
OD2
|
F:ASP145
|
4.1
|
23.0
|
0.5
|
O3A
|
F:ATP301
|
4.1
|
21.3
|
1.0
|
O1B
|
F:ATP301
|
4.2
|
20.8
|
1.0
|
O
|
F:HOH506
|
4.2
|
29.8
|
1.0
|
OD1
|
F:ASP145
|
4.3
|
29.1
|
0.6
|
OD1
|
F:ASP145
|
4.3
|
26.1
|
0.5
|
CG2
|
F:THR53
|
4.3
|
24.4
|
1.0
|
O
|
F:HOH435
|
4.3
|
37.0
|
1.0
|
NE
|
A:ARG226
|
4.5
|
24.5
|
1.0
|
PA
|
F:ATP301
|
4.5
|
26.8
|
1.0
|
NH2
|
A:ARG226
|
4.5
|
21.9
|
1.0
|
O1G
|
F:ATP301
|
4.5
|
38.1
|
1.0
|
CG
|
F:ASP145
|
4.6
|
27.8
|
0.6
|
CG
|
F:ASP145
|
4.6
|
26.7
|
0.5
|
O2A
|
F:ATP301
|
4.7
|
30.6
|
1.0
|
CZ
|
A:ARG226
|
4.9
|
25.2
|
1.0
|
CB
|
F:LYS52
|
4.9
|
20.1
|
1.0
|
C
|
F:LYS52
|
5.0
|
24.6
|
1.0
|
|
Reference:
J.Abe,
T.B.Hiyama,
A.Mukaiyama,
S.Son,
T.Mori,
S.Saito,
M.Osako,
J.Wolanin,
E.Yamashita,
T.Kondo,
S.Akiyama.
Circadian Rhythms. Atomic-Scale Origins of Slowness in the Cyanobacterial Circadian Clock. Science V. 349 312 2015.
ISSN: ESSN 1095-9203
PubMed: 26113637
DOI: 10.1126/SCIENCE.1261040
Page generated: Tue Aug 20 03:45:27 2024
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