Magnesium in PDB 1rlo: Phospho-Aspartyl Intermediate Analogue of Ybiv From E. Coli K12
Protein crystallography data
The structure of Phospho-Aspartyl Intermediate Analogue of Ybiv From E. Coli K12, PDB code: 1rlo
was solved by
A.Roberts,
S.Y.Lee,
E.Mccullagh,
R.E.Silversmith,
D.E.Wemmer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.85 /
2.00
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
71.276,
91.195,
176.415,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21.9 /
25.1
|
Other elements in 1rlo:
The structure of Phospho-Aspartyl Intermediate Analogue of Ybiv From E. Coli K12 also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Phospho-Aspartyl Intermediate Analogue of Ybiv From E. Coli K12
(pdb code 1rlo). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Phospho-Aspartyl Intermediate Analogue of Ybiv From E. Coli K12, PDB code: 1rlo:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 1rlo
Go back to
Magnesium Binding Sites List in 1rlo
Magnesium binding site 1 out
of 4 in the Phospho-Aspartyl Intermediate Analogue of Ybiv From E. Coli K12
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Phospho-Aspartyl Intermediate Analogue of Ybiv From E. Coli K12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg801
b:11.3
occ:1.00
|
OD2
|
A:BFD9
|
2.0
|
10.4
|
1.0
|
OD1
|
A:ASP215
|
2.0
|
12.1
|
1.0
|
O
|
A:ASP11
|
2.0
|
13.7
|
1.0
|
F2
|
A:BFD9
|
2.1
|
11.1
|
1.0
|
O
|
A:HOH927
|
2.1
|
10.8
|
1.0
|
O
|
A:HOH802
|
2.2
|
13.7
|
1.0
|
CG
|
A:BFD9
|
2.9
|
10.6
|
1.0
|
CG
|
A:ASP215
|
3.0
|
15.4
|
1.0
|
BE
|
A:BFD9
|
3.1
|
12.9
|
1.0
|
C
|
A:ASP11
|
3.2
|
13.3
|
1.0
|
OD1
|
A:BFD9
|
3.3
|
12.0
|
1.0
|
OD2
|
A:ASP215
|
3.3
|
14.4
|
1.0
|
CA
|
A:ASP11
|
4.0
|
13.1
|
1.0
|
OG1
|
A:THR13
|
4.0
|
13.9
|
1.0
|
OD2
|
A:ASP219
|
4.0
|
12.4
|
1.0
|
O
|
A:GLY179
|
4.1
|
16.6
|
1.0
|
F1
|
A:BFD9
|
4.1
|
12.8
|
1.0
|
N
|
A:ASP11
|
4.1
|
10.2
|
1.0
|
OG
|
A:SER216
|
4.1
|
25.4
|
1.0
|
CB
|
A:ASP11
|
4.1
|
13.7
|
1.0
|
CB
|
A:BFD9
|
4.2
|
9.5
|
1.0
|
F3
|
A:BFD9
|
4.2
|
12.5
|
1.0
|
N
|
A:GLY12
|
4.3
|
13.8
|
1.0
|
CB
|
A:ASP215
|
4.4
|
15.3
|
1.0
|
CA
|
A:GLY179
|
4.4
|
16.9
|
1.0
|
CA
|
A:GLY12
|
4.5
|
14.0
|
1.0
|
N
|
A:SER216
|
4.5
|
17.7
|
1.0
|
CB
|
A:SER216
|
4.6
|
20.8
|
1.0
|
N
|
A:ASP215
|
4.6
|
18.0
|
1.0
|
C
|
A:GLY12
|
4.6
|
13.5
|
1.0
|
C
|
A:MET10
|
4.7
|
10.1
|
1.0
|
C
|
A:GLY179
|
4.7
|
18.4
|
1.0
|
N
|
A:THR13
|
4.7
|
13.9
|
1.0
|
OD1
|
A:ASN218
|
4.7
|
21.2
|
1.0
|
N
|
A:MET10
|
4.8
|
11.3
|
1.0
|
CB
|
A:THR13
|
4.9
|
14.3
|
1.0
|
CA
|
A:ASP215
|
4.9
|
16.8
|
1.0
|
C
|
A:BFD9
|
4.9
|
12.7
|
1.0
|
CG
|
A:ASP219
|
5.0
|
12.7
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 1rlo
Go back to
Magnesium Binding Sites List in 1rlo
Magnesium binding site 2 out
of 4 in the Phospho-Aspartyl Intermediate Analogue of Ybiv From E. Coli K12
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Phospho-Aspartyl Intermediate Analogue of Ybiv From E. Coli K12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg802
b:12.0
occ:1.00
|
OD2
|
B:BFD9
|
2.0
|
13.9
|
1.0
|
OD1
|
B:ASP215
|
2.0
|
16.0
|
1.0
|
O
|
B:HOH899
|
2.0
|
9.9
|
1.0
|
F2
|
B:BFD9
|
2.0
|
14.0
|
1.0
|
O
|
B:ASP11
|
2.0
|
13.4
|
1.0
|
O
|
B:HOH805
|
2.1
|
16.2
|
1.0
|
CG
|
B:BFD9
|
2.9
|
16.4
|
1.0
|
CG
|
B:ASP215
|
3.1
|
20.1
|
1.0
|
BE
|
B:BFD9
|
3.2
|
14.7
|
1.0
|
C
|
B:ASP11
|
3.2
|
14.5
|
1.0
|
OD1
|
B:BFD9
|
3.3
|
15.9
|
1.0
|
OD2
|
B:ASP215
|
3.4
|
19.1
|
1.0
|
OG
|
B:SER216
|
3.8
|
30.0
|
1.0
|
CA
|
B:ASP11
|
4.0
|
14.0
|
1.0
|
OD2
|
B:ASP219
|
4.0
|
17.4
|
1.0
|
CB
|
B:ASP11
|
4.0
|
13.6
|
1.0
|
O
|
B:GLY179
|
4.0
|
37.0
|
1.0
|
OG1
|
B:THR13
|
4.1
|
12.5
|
1.0
|
F1
|
B:BFD9
|
4.1
|
14.2
|
1.0
|
N
|
B:ASP11
|
4.1
|
13.5
|
1.0
|
F3
|
B:BFD9
|
4.2
|
13.4
|
1.0
|
CB
|
B:BFD9
|
4.2
|
15.7
|
1.0
|
N
|
B:GLY12
|
4.3
|
13.4
|
1.0
|
CB
|
B:ASP215
|
4.4
|
18.4
|
1.0
|
CA
|
B:GLY179
|
4.4
|
36.9
|
1.0
|
CA
|
B:GLY12
|
4.5
|
14.0
|
1.0
|
N
|
B:SER216
|
4.6
|
19.1
|
1.0
|
C
|
B:GLY12
|
4.6
|
15.2
|
1.0
|
OD1
|
B:ASN218
|
4.7
|
19.9
|
1.0
|
N
|
B:ASP215
|
4.7
|
16.1
|
1.0
|
CB
|
B:SER216
|
4.7
|
23.8
|
1.0
|
N
|
B:THR13
|
4.7
|
15.4
|
1.0
|
C
|
B:GLY179
|
4.7
|
38.0
|
1.0
|
C
|
B:MET10
|
4.8
|
13.8
|
1.0
|
CB
|
B:THR13
|
4.9
|
12.2
|
1.0
|
N
|
B:MET10
|
4.9
|
14.4
|
1.0
|
CA
|
B:ASP215
|
4.9
|
18.8
|
1.0
|
CG
|
B:ASP219
|
5.0
|
17.5
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 1rlo
Go back to
Magnesium Binding Sites List in 1rlo
Magnesium binding site 3 out
of 4 in the Phospho-Aspartyl Intermediate Analogue of Ybiv From E. Coli K12
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Phospho-Aspartyl Intermediate Analogue of Ybiv From E. Coli K12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg803
b:22.7
occ:1.00
|
O
|
C:HOH912
|
2.0
|
16.3
|
1.0
|
O
|
C:HOH891
|
2.0
|
16.1
|
1.0
|
O
|
C:ASP11
|
2.1
|
23.0
|
1.0
|
F2
|
C:BFD9
|
2.1
|
18.3
|
1.0
|
OD1
|
C:ASP215
|
2.1
|
21.8
|
1.0
|
OD2
|
C:BFD9
|
2.2
|
14.8
|
1.0
|
CG
|
C:BFD9
|
3.1
|
17.9
|
1.0
|
CG
|
C:ASP215
|
3.1
|
24.6
|
1.0
|
BE
|
C:BFD9
|
3.2
|
17.3
|
1.0
|
C
|
C:ASP11
|
3.3
|
23.5
|
1.0
|
OD1
|
C:BFD9
|
3.4
|
14.2
|
1.0
|
OD2
|
C:ASP215
|
3.4
|
25.3
|
1.0
|
O
|
C:SER178
|
3.9
|
21.6
|
1.0
|
OD2
|
C:ASP219
|
4.0
|
16.3
|
1.0
|
OG1
|
C:THR13
|
4.0
|
23.2
|
1.0
|
CA
|
C:ASP11
|
4.0
|
22.4
|
1.0
|
F1
|
C:BFD9
|
4.0
|
14.0
|
1.0
|
OG
|
C:SER216
|
4.0
|
31.8
|
1.0
|
CB
|
C:ASP11
|
4.1
|
26.4
|
1.0
|
N
|
C:ASP11
|
4.2
|
19.8
|
1.0
|
N
|
C:GLY12
|
4.3
|
24.8
|
1.0
|
F3
|
C:BFD9
|
4.3
|
19.6
|
1.0
|
CB
|
C:BFD9
|
4.4
|
16.3
|
1.0
|
CB
|
C:SER216
|
4.5
|
25.9
|
1.0
|
CA
|
C:GLY12
|
4.5
|
24.1
|
1.0
|
CB
|
C:ASP215
|
4.5
|
22.8
|
1.0
|
N
|
C:SER216
|
4.6
|
22.3
|
1.0
|
OD1
|
C:ASN218
|
4.6
|
18.5
|
1.0
|
C
|
C:GLY12
|
4.6
|
24.9
|
1.0
|
N
|
C:ASP215
|
4.8
|
22.8
|
1.0
|
C
|
C:MET10
|
4.8
|
20.6
|
1.0
|
O
|
C:HOH875
|
4.8
|
28.5
|
1.0
|
N
|
C:THR13
|
4.8
|
24.5
|
1.0
|
O
|
C:HOH900
|
4.8
|
45.5
|
1.0
|
CB
|
C:THR13
|
4.9
|
24.1
|
1.0
|
CG
|
C:ASP219
|
4.9
|
16.6
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 1rlo
Go back to
Magnesium Binding Sites List in 1rlo
Magnesium binding site 4 out
of 4 in the Phospho-Aspartyl Intermediate Analogue of Ybiv From E. Coli K12
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Phospho-Aspartyl Intermediate Analogue of Ybiv From E. Coli K12 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg804
b:12.5
occ:1.00
|
OD1
|
D:ASP215
|
2.0
|
11.7
|
1.0
|
O
|
D:HOH895
|
2.0
|
13.9
|
1.0
|
O
|
D:HOH896
|
2.1
|
12.5
|
1.0
|
F2
|
D:BFD9
|
2.1
|
12.9
|
1.0
|
O
|
D:ASP11
|
2.1
|
10.3
|
1.0
|
OD2
|
D:BFD9
|
2.1
|
13.5
|
1.0
|
CG
|
D:BFD9
|
3.0
|
16.2
|
1.0
|
CG
|
D:ASP215
|
3.0
|
13.6
|
1.0
|
BE
|
D:BFD9
|
3.2
|
14.8
|
1.0
|
C
|
D:ASP11
|
3.2
|
13.5
|
1.0
|
OD1
|
D:BFD9
|
3.4
|
13.0
|
1.0
|
OD2
|
D:ASP215
|
3.4
|
13.2
|
1.0
|
OD2
|
D:ASP219
|
3.9
|
12.0
|
1.0
|
CA
|
D:ASP11
|
4.0
|
13.0
|
1.0
|
O
|
D:SER178
|
4.0
|
23.3
|
1.0
|
CB
|
D:ASP11
|
4.0
|
14.9
|
1.0
|
OG1
|
D:THR13
|
4.1
|
11.3
|
1.0
|
F1
|
D:BFD9
|
4.1
|
13.1
|
1.0
|
N
|
D:ASP11
|
4.1
|
13.0
|
1.0
|
F3
|
D:BFD9
|
4.2
|
15.3
|
1.0
|
N
|
D:GLY12
|
4.3
|
14.3
|
1.0
|
OG
|
D:SER216
|
4.3
|
23.5
|
1.0
|
CB
|
D:BFD9
|
4.3
|
14.9
|
1.0
|
CB
|
D:ASP215
|
4.4
|
10.3
|
1.0
|
CA
|
D:GLY12
|
4.5
|
14.1
|
1.0
|
CB
|
D:SER216
|
4.5
|
16.7
|
1.0
|
N
|
D:SER216
|
4.5
|
14.6
|
1.0
|
OD1
|
D:ASN218
|
4.7
|
18.0
|
1.0
|
C
|
D:GLY12
|
4.7
|
14.4
|
1.0
|
N
|
D:ASP215
|
4.7
|
11.7
|
1.0
|
C
|
D:MET10
|
4.8
|
13.6
|
1.0
|
N
|
D:THR13
|
4.8
|
13.5
|
1.0
|
O
|
D:HOH840
|
4.8
|
33.0
|
1.0
|
CG
|
D:ASP219
|
4.9
|
14.6
|
1.0
|
CA
|
D:ASP215
|
5.0
|
14.0
|
1.0
|
N
|
D:MET10
|
5.0
|
14.0
|
1.0
|
|
Reference:
A.Roberts,
S.Y.Lee,
E.Mccullagh,
R.E.Silversmith,
D.E.Wemmer.
Ybiv From Escherichia Coli K12 Is A Had Phosphatase. Proteins V. 58 790 2005.
ISSN: ISSN 0887-3585
PubMed: 15657928
DOI: 10.1002/PROT.20267
Page generated: Tue Aug 13 13:03:20 2024
|