Magnesium in PDB 2ce7: Edta Treated
Protein crystallography data
The structure of Edta Treated, PDB code: 2ce7
was solved by
C.Bieniossek,
U.Baumann,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
25.00 /
2.44
|
Space group
|
P 41 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
165.092,
165.092,
235.322,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
22.2 /
26.9
|
Other elements in 2ce7:
The structure of Edta Treated also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Edta Treated
(pdb code 2ce7). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 6 binding sites of Magnesium where determined in the
Edta Treated, PDB code: 2ce7:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
Magnesium binding site 1 out
of 6 in 2ce7
Go back to
Magnesium Binding Sites List in 2ce7
Magnesium binding site 1 out
of 6 in the Edta Treated
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Edta Treated within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1605
b:33.4
occ:1.00
|
O
|
A:HOH2046
|
2.0
|
21.9
|
1.0
|
O2B
|
A:ADP1604
|
2.2
|
20.8
|
1.0
|
PB
|
A:ADP1604
|
3.5
|
19.1
|
1.0
|
O3B
|
A:ADP1604
|
3.7
|
19.1
|
1.0
|
O2A
|
A:ADP1604
|
3.8
|
22.6
|
1.0
|
O
|
A:HOH2006
|
3.8
|
31.3
|
1.0
|
OD1
|
A:ASP260
|
4.3
|
36.1
|
1.0
|
N
|
A:GLY204
|
4.4
|
27.2
|
1.0
|
O3A
|
A:ADP1604
|
4.4
|
21.2
|
1.0
|
NZ
|
A:LYS207
|
4.4
|
28.3
|
1.0
|
O1B
|
A:ADP1604
|
4.6
|
21.0
|
1.0
|
CA
|
A:PRO203
|
4.6
|
28.2
|
1.0
|
CB
|
A:PRO203
|
4.7
|
27.0
|
1.0
|
OD2
|
A:ASP260
|
4.7
|
36.0
|
1.0
|
PA
|
A:ADP1604
|
4.7
|
17.3
|
1.0
|
OG1
|
A:THR208
|
4.8
|
24.0
|
1.0
|
CG
|
A:ASP260
|
5.0
|
35.2
|
1.0
|
|
Magnesium binding site 2 out
of 6 in 2ce7
Go back to
Magnesium Binding Sites List in 2ce7
Magnesium binding site 2 out
of 6 in the Edta Treated
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Edta Treated within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1608
b:34.4
occ:1.00
|
O
|
B:HOH2033
|
2.1
|
31.1
|
1.0
|
O2B
|
B:ADP1607
|
2.2
|
14.9
|
1.0
|
PB
|
B:ADP1607
|
3.3
|
10.7
|
1.0
|
O
|
B:HOH2004
|
3.3
|
14.4
|
1.0
|
O3B
|
B:ADP1607
|
3.5
|
8.9
|
1.0
|
NZ
|
B:LYS207
|
3.9
|
30.2
|
1.0
|
O2A
|
B:ADP1607
|
4.2
|
24.5
|
1.0
|
OD1
|
B:ASP260
|
4.2
|
36.6
|
1.0
|
OD2
|
B:ASP260
|
4.3
|
41.2
|
1.0
|
O1B
|
B:ADP1607
|
4.4
|
14.8
|
1.0
|
N
|
B:GLY204
|
4.4
|
27.7
|
1.0
|
O3A
|
B:ADP1607
|
4.4
|
16.6
|
1.0
|
CA
|
B:PRO203
|
4.5
|
27.9
|
1.0
|
CB
|
B:PRO203
|
4.7
|
26.9
|
1.0
|
CG
|
B:ASP260
|
4.7
|
33.5
|
1.0
|
OG1
|
B:THR208
|
4.7
|
25.5
|
1.0
|
C
|
B:PRO203
|
5.0
|
27.2
|
1.0
|
|
Magnesium binding site 3 out
of 6 in 2ce7
Go back to
Magnesium Binding Sites List in 2ce7
Magnesium binding site 3 out
of 6 in the Edta Treated
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Edta Treated within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1609
b:50.4
occ:1.00
|
O2B
|
C:ADP1608
|
2.2
|
48.7
|
1.0
|
CB
|
C:PRO203
|
3.5
|
27.6
|
1.0
|
PB
|
C:ADP1608
|
3.5
|
47.2
|
1.0
|
CA
|
C:PRO203
|
3.6
|
28.7
|
1.0
|
N
|
C:GLY204
|
3.9
|
27.8
|
1.0
|
O3B
|
C:ADP1608
|
3.9
|
46.6
|
1.0
|
NZ
|
C:LYS207
|
4.0
|
31.6
|
1.0
|
C
|
C:PRO203
|
4.2
|
28.2
|
1.0
|
O1B
|
C:ADP1608
|
4.3
|
51.9
|
1.0
|
O2A
|
C:ADP1608
|
4.4
|
52.0
|
1.0
|
O3A
|
C:ADP1608
|
4.6
|
49.4
|
1.0
|
CE
|
C:LYS207
|
4.7
|
29.6
|
1.0
|
N
|
C:PRO203
|
4.8
|
28.1
|
1.0
|
CG
|
C:PRO203
|
4.9
|
28.1
|
1.0
|
|
Magnesium binding site 4 out
of 6 in 2ce7
Go back to
Magnesium Binding Sites List in 2ce7
Magnesium binding site 4 out
of 6 in the Edta Treated
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Edta Treated within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg1609
b:34.0
occ:1.00
|
O
|
D:HOH2031
|
1.6
|
32.3
|
1.0
|
O2B
|
D:ADP1608
|
2.2
|
15.8
|
1.0
|
O2A
|
D:ADP1608
|
2.2
|
21.9
|
1.0
|
O
|
D:HOH2032
|
2.3
|
20.5
|
1.0
|
O
|
D:HOH2033
|
2.9
|
31.4
|
1.0
|
PB
|
D:ADP1608
|
3.0
|
12.6
|
1.0
|
O3B
|
D:ADP1608
|
3.2
|
9.0
|
1.0
|
PA
|
D:ADP1608
|
3.2
|
12.6
|
1.0
|
O3A
|
D:ADP1608
|
3.3
|
14.0
|
1.0
|
O
|
D:HOH2008
|
3.5
|
23.6
|
1.0
|
O5'
|
D:ADP1608
|
3.6
|
14.0
|
1.0
|
O
|
D:HOH2007
|
3.7
|
19.8
|
1.0
|
OG1
|
D:THR208
|
3.9
|
25.4
|
1.0
|
O1B
|
D:ADP1608
|
4.4
|
6.9
|
1.0
|
N
|
D:GLY204
|
4.5
|
27.6
|
1.0
|
O1A
|
D:ADP1608
|
4.6
|
15.6
|
1.0
|
CB
|
D:THR208
|
4.8
|
30.2
|
1.0
|
CA
|
D:GLY204
|
4.8
|
27.0
|
1.0
|
C5'
|
D:ADP1608
|
4.8
|
17.8
|
1.0
|
|
Magnesium binding site 5 out
of 6 in 2ce7
Go back to
Magnesium Binding Sites List in 2ce7
Magnesium binding site 5 out
of 6 in the Edta Treated
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Edta Treated within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg1605
b:35.1
occ:1.00
|
O2B
|
E:ADP1604
|
2.2
|
27.4
|
1.0
|
O2A
|
E:ADP1604
|
2.2
|
28.7
|
1.0
|
O
|
E:HOH2037
|
2.3
|
24.1
|
1.0
|
O
|
E:HOH2038
|
2.3
|
26.1
|
1.0
|
O
|
E:HOH2036
|
2.4
|
27.1
|
1.0
|
PB
|
E:ADP1604
|
3.1
|
24.0
|
1.0
|
O3B
|
E:ADP1604
|
3.3
|
22.1
|
1.0
|
PA
|
E:ADP1604
|
3.3
|
20.0
|
1.0
|
O3A
|
E:ADP1604
|
3.4
|
22.6
|
1.0
|
O5'
|
E:ADP1604
|
3.8
|
21.9
|
1.0
|
OG1
|
E:THR208
|
4.1
|
27.9
|
1.0
|
N
|
E:GLY204
|
4.4
|
27.4
|
1.0
|
O1B
|
E:ADP1604
|
4.5
|
20.8
|
1.0
|
O1A
|
E:ADP1604
|
4.7
|
20.3
|
1.0
|
OD1
|
E:ASP260
|
4.7
|
33.5
|
1.0
|
CA
|
E:GLY204
|
4.8
|
27.9
|
1.0
|
OD2
|
E:ASP260
|
4.9
|
31.8
|
1.0
|
CB
|
E:THR208
|
5.0
|
28.4
|
1.0
|
|
Magnesium binding site 6 out
of 6 in 2ce7
Go back to
Magnesium Binding Sites List in 2ce7
Magnesium binding site 6 out
of 6 in the Edta Treated
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Edta Treated within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg1608
b:44.2
occ:1.00
|
O2B
|
F:ADP1607
|
2.2
|
53.2
|
1.0
|
O2A
|
F:ADP1607
|
2.8
|
60.1
|
1.0
|
O3B
|
F:ADP1607
|
3.0
|
54.6
|
1.0
|
PB
|
F:ADP1607
|
3.0
|
56.1
|
1.0
|
O3A
|
F:ADP1607
|
3.7
|
58.1
|
1.0
|
O
|
F:HOH2001
|
3.8
|
31.7
|
1.0
|
PA
|
F:ADP1607
|
3.8
|
63.6
|
1.0
|
N
|
F:GLY204
|
4.3
|
27.8
|
1.0
|
OG1
|
F:THR208
|
4.3
|
27.4
|
1.0
|
OD1
|
F:ASP260
|
4.4
|
29.7
|
1.0
|
O1B
|
F:ADP1607
|
4.4
|
49.2
|
1.0
|
O1A
|
F:ADP1607
|
4.6
|
63.6
|
1.0
|
CA
|
F:PRO203
|
4.9
|
28.4
|
1.0
|
OD2
|
F:ASP260
|
4.9
|
31.9
|
1.0
|
|
Reference:
C.Bieniossek,
T.Schalch,
M.Bumann,
M.Meister,
R.Meier,
U.Baumann.
The Molecular Architecture of the Metalloprotease Ftsh. Proc.Natl.Acad.Sci.Usa V. 103 3066 2006.
ISSN: ISSN 0027-8424
PubMed: 16484367
DOI: 10.1073/PNAS.0600031103
Page generated: Tue Aug 13 22:14:58 2024
|