Magnesium in PDB 1s1m: Crystal Structure of E. Coli Ctp Synthetase
Enzymatic activity of Crystal Structure of E. Coli Ctp Synthetase
All present enzymatic activity of Crystal Structure of E. Coli Ctp Synthetase:
6.3.4.2;
Protein crystallography data
The structure of Crystal Structure of E. Coli Ctp Synthetase, PDB code: 1s1m
was solved by
J.A.Endrizzi,
H.Kim,
P.M.Anderson,
E.P.Baldwin,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
2.30
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
165.507,
106.807,
130.033,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
n/a /
n/a
|
Other elements in 1s1m:
The structure of Crystal Structure of E. Coli Ctp Synthetase also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of E. Coli Ctp Synthetase
(pdb code 1s1m). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Crystal Structure of E. Coli Ctp Synthetase, PDB code: 1s1m:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 1s1m
Go back to
Magnesium Binding Sites List in 1s1m
Magnesium binding site 1 out
of 4 in the Crystal Structure of E. Coli Ctp Synthetase
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 E. Coli Ctp Synthetase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg702
b:48.0
occ:1.00
|
OE2
|
A:GLU140
|
2.3
|
45.2
|
1.0
|
OD2
|
A:ASP72
|
2.5
|
45.6
|
1.0
|
O3
|
A:SO4603
|
2.8
|
68.8
|
1.0
|
O1
|
A:SO4602
|
2.9
|
82.3
|
1.0
|
O2
|
A:SO4602
|
3.1
|
88.0
|
1.0
|
CG
|
A:ASP72
|
3.3
|
49.3
|
1.0
|
CD
|
A:GLU140
|
3.3
|
51.3
|
1.0
|
OD1
|
A:ASP72
|
3.4
|
48.0
|
1.0
|
S
|
A:SO4602
|
3.4
|
72.8
|
1.0
|
N
|
A:GLY19
|
3.5
|
30.7
|
1.0
|
OE1
|
A:GLU140
|
3.6
|
50.4
|
1.0
|
NZ
|
A:LYS40
|
3.6
|
34.5
|
1.0
|
O3
|
A:SO4602
|
3.7
|
75.2
|
1.0
|
CA
|
A:GLY19
|
3.8
|
34.5
|
1.0
|
O2
|
A:SO4603
|
3.8
|
90.4
|
1.0
|
CE
|
A:LYS40
|
3.8
|
29.4
|
1.0
|
S
|
A:SO4603
|
3.8
|
86.3
|
1.0
|
O
|
A:HOH970
|
3.9
|
69.8
|
1.0
|
NZ
|
A:LYS18
|
4.0
|
47.4
|
1.0
|
O
|
A:HOH889
|
4.0
|
72.9
|
1.0
|
C
|
A:LYS18
|
4.4
|
39.3
|
1.0
|
CB
|
A:LYS18
|
4.4
|
35.6
|
1.0
|
O1
|
A:SO4603
|
4.5
|
83.3
|
1.0
|
CB
|
A:ASP72
|
4.6
|
43.3
|
1.0
|
CG
|
A:GLU140
|
4.6
|
48.4
|
1.0
|
CE
|
A:LYS18
|
4.7
|
51.1
|
1.0
|
CD
|
A:LYS40
|
4.7
|
34.4
|
1.0
|
O4
|
A:SO4602
|
4.8
|
65.8
|
1.0
|
CA
|
A:LYS18
|
4.8
|
38.5
|
1.0
|
O
|
A:HOH908
|
4.9
|
49.0
|
1.0
|
N
|
A:LYS18
|
5.0
|
41.0
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 1s1m
Go back to
Magnesium Binding Sites List in 1s1m
Magnesium binding site 2 out
of 4 in the Crystal Structure of E. Coli Ctp Synthetase
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 E. Coli Ctp Synthetase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg703
b:92.0
occ:1.00
|
O4
|
A:SO4603
|
2.1
|
91.0
|
1.0
|
OD1
|
A:ASP42
|
2.3
|
42.4
|
1.0
|
CG
|
A:ASP42
|
3.3
|
41.0
|
1.0
|
S
|
A:SO4603
|
3.3
|
86.3
|
1.0
|
CD
|
A:PRO43
|
3.7
|
33.3
|
1.0
|
O2
|
A:SO4603
|
3.7
|
90.4
|
1.0
|
NZ
|
A:LYS40
|
3.7
|
34.5
|
1.0
|
CB
|
A:ASP42
|
3.8
|
31.0
|
1.0
|
O3
|
A:SO4603
|
3.8
|
68.8
|
1.0
|
CA
|
A:ASP42
|
3.8
|
30.6
|
1.0
|
CA
|
A:GLY142
|
3.8
|
36.1
|
1.0
|
CE2
|
A:TYR44
|
4.1
|
54.4
|
1.0
|
CE
|
A:LYS40
|
4.1
|
29.4
|
1.0
|
O
|
A:HOH872
|
4.2
|
53.9
|
1.0
|
N
|
A:GLY143
|
4.2
|
43.2
|
1.0
|
CD2
|
A:TYR44
|
4.4
|
50.8
|
1.0
|
OD2
|
A:ASP42
|
4.4
|
50.2
|
1.0
|
C
|
A:GLY142
|
4.4
|
43.1
|
1.0
|
O1
|
A:SO4603
|
4.5
|
83.3
|
1.0
|
N
|
A:PRO43
|
4.6
|
40.9
|
1.0
|
C
|
A:ASP42
|
4.6
|
44.3
|
1.0
|
CG
|
A:PRO43
|
4.7
|
39.3
|
1.0
|
O
|
A:LEU41
|
4.8
|
34.9
|
1.0
|
N
|
A:ASP42
|
4.9
|
31.5
|
1.0
|
N
|
A:GLY142
|
5.0
|
36.1
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 1s1m
Go back to
Magnesium Binding Sites List in 1s1m
Magnesium binding site 3 out
of 4 in the Crystal Structure of E. Coli Ctp Synthetase
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 E. Coli Ctp Synthetase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg701
b:64.4
occ:1.00
|
O3
|
B:SO41602
|
2.4
|
61.1
|
1.0
|
OE2
|
B:GLU140
|
2.6
|
56.8
|
1.0
|
OD1
|
B:ASP72
|
2.6
|
51.5
|
1.0
|
O
|
B:HOH1690
|
3.2
|
53.1
|
1.0
|
O4
|
B:SO41603
|
3.2
|
57.3
|
1.0
|
CG
|
B:ASP72
|
3.2
|
49.9
|
1.0
|
S
|
B:SO41602
|
3.4
|
89.8
|
1.0
|
OD2
|
B:ASP72
|
3.4
|
48.6
|
1.0
|
N
|
B:GLY19
|
3.5
|
32.9
|
1.0
|
O2
|
B:SO41602
|
3.5
|
54.8
|
1.0
|
O2
|
B:SO41603
|
3.5
|
65.2
|
1.0
|
CD
|
B:GLU140
|
3.6
|
53.4
|
1.0
|
CA
|
B:GLY19
|
3.7
|
33.4
|
1.0
|
O4
|
B:SO41602
|
3.7
|
70.2
|
1.0
|
OE1
|
B:GLU140
|
3.7
|
62.2
|
1.0
|
S
|
B:SO41603
|
4.0
|
78.7
|
1.0
|
CE
|
B:LYS40
|
4.1
|
32.5
|
1.0
|
NZ
|
B:LYS40
|
4.2
|
33.9
|
1.0
|
O
|
B:HOH1753
|
4.2
|
68.8
|
1.0
|
NZ
|
B:LYS18
|
4.3
|
50.6
|
1.0
|
CB
|
B:LYS18
|
4.3
|
41.9
|
1.0
|
C
|
B:LYS18
|
4.4
|
38.5
|
1.0
|
CB
|
B:ASP72
|
4.5
|
43.4
|
1.0
|
O
|
B:HOH1688
|
4.6
|
54.4
|
1.0
|
O1
|
B:SO41602
|
4.7
|
60.2
|
1.0
|
CD
|
B:LYS40
|
4.8
|
37.6
|
1.0
|
CE
|
B:LYS18
|
4.9
|
34.1
|
1.0
|
CA
|
B:LYS18
|
4.9
|
40.3
|
1.0
|
CG
|
B:GLU140
|
4.9
|
41.0
|
1.0
|
O3
|
B:SO41603
|
4.9
|
92.0
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 1s1m
Go back to
Magnesium Binding Sites List in 1s1m
Magnesium binding site 4 out
of 4 in the Crystal Structure of E. Coli Ctp Synthetase
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 E. Coli Ctp Synthetase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg704
b:91.0
occ:1.00
|
O1
|
B:SO41603
|
2.1
|
93.0
|
1.0
|
OD1
|
B:ASP42
|
2.9
|
41.9
|
1.0
|
S
|
B:SO41603
|
3.3
|
78.7
|
1.0
|
O2
|
B:SO41603
|
3.4
|
65.2
|
1.0
|
NZ
|
B:LYS40
|
3.6
|
33.9
|
1.0
|
CG
|
B:ASP42
|
3.7
|
40.1
|
1.0
|
CD
|
B:PRO43
|
3.8
|
42.8
|
1.0
|
CA
|
B:GLY142
|
4.1
|
37.1
|
1.0
|
O3
|
B:SO41603
|
4.1
|
92.0
|
1.0
|
N
|
B:GLY143
|
4.1
|
50.9
|
1.0
|
CE2
|
B:TYR44
|
4.2
|
44.4
|
1.0
|
CB
|
B:ASP42
|
4.2
|
31.5
|
1.0
|
CE
|
B:LYS40
|
4.3
|
32.5
|
1.0
|
O4
|
B:SO41603
|
4.3
|
57.3
|
1.0
|
CA
|
B:ASP42
|
4.3
|
33.3
|
1.0
|
CD2
|
B:TYR44
|
4.5
|
47.1
|
1.0
|
C
|
B:GLY142
|
4.6
|
50.6
|
1.0
|
CG
|
B:PRO43
|
4.7
|
49.0
|
1.0
|
N
|
B:PRO43
|
4.7
|
40.4
|
1.0
|
OD2
|
B:ASP42
|
4.8
|
44.3
|
1.0
|
C
|
B:ASP42
|
5.0
|
41.3
|
1.0
|
OD1
|
B:ASP70
|
5.0
|
74.2
|
1.0
|
|
Reference:
J.A.Endrizzi,
H.Kim,
P.M.Anderson,
E.P.Baldwin.
Crystal Structure of Escherichia Coli Cytidine Triphosphate Synthetase, A Nucleotide-Regulated Glutamine Amidotransferase/Atp-Dependent Amidoligase Fusion Protein and Homologue of Anticancer and Antiparasitic Drug Targets Biochemistry V. 43 6447 2004.
ISSN: ISSN 0006-2960
PubMed: 15157079
DOI: 10.1021/BI0496945
Page generated: Tue Aug 13 13:14:08 2024
|