Magnesium in PDB 3rv0: Crystal Structure of K. Polysporus DCR1 Without the C-Terminal Dsrbd
Protein crystallography data
The structure of Crystal Structure of K. Polysporus DCR1 Without the C-Terminal Dsrbd, PDB code: 3rv0
was solved by
K.Nakanishi,
D.E.Weinberg,
D.P.Bartel,
D.J.Patel,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
43.41 /
2.29
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
101.037,
112.974,
135.689,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.5 /
22
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of K. Polysporus DCR1 Without the C-Terminal Dsrbd
(pdb code 3rv0). 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 K. Polysporus DCR1 Without the C-Terminal Dsrbd, PDB code: 3rv0:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 3rv0
Go back to
Magnesium Binding Sites List in 3rv0
Magnesium binding site 1 out
of 4 in the Crystal Structure of K. Polysporus DCR1 Without the C-Terminal Dsrbd
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 K. Polysporus DCR1 Without the C-Terminal Dsrbd within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1
b:45.4
occ:1.00
|
O
|
A:HOH363
|
2.1
|
34.6
|
1.0
|
O
|
A:HOH389
|
2.1
|
46.1
|
1.0
|
O
|
A:HOH372
|
2.2
|
40.3
|
1.0
|
OE1
|
A:GLU224
|
2.2
|
37.8
|
1.0
|
O
|
A:HOH379
|
2.3
|
41.1
|
1.0
|
OE2
|
A:GLU147
|
2.3
|
60.1
|
1.0
|
CD
|
A:GLU224
|
3.2
|
38.3
|
1.0
|
CD
|
A:GLU147
|
3.4
|
57.9
|
1.0
|
OE2
|
A:GLU224
|
3.4
|
43.1
|
1.0
|
NZ
|
A:LYS217
|
3.7
|
79.5
|
1.0
|
OD1
|
A:ASP221
|
3.7
|
61.6
|
1.0
|
CG
|
A:GLU147
|
3.8
|
41.3
|
1.0
|
O
|
A:HOH444
|
3.9
|
45.1
|
1.0
|
O
|
A:HOH469
|
4.0
|
54.8
|
1.0
|
O
|
A:HOH424
|
4.2
|
52.0
|
1.0
|
OD2
|
A:ASP151
|
4.3
|
44.3
|
1.0
|
OD1
|
A:ASN184
|
4.4
|
57.8
|
1.0
|
OE1
|
A:GLU147
|
4.4
|
58.1
|
1.0
|
CG
|
A:GLU224
|
4.5
|
35.5
|
1.0
|
CE
|
A:LYS217
|
4.7
|
77.3
|
1.0
|
CG
|
A:ASP221
|
4.7
|
56.7
|
1.0
|
CG
|
A:ASP151
|
4.8
|
38.9
|
1.0
|
CB
|
A:ASP151
|
4.9
|
28.3
|
1.0
|
CA
|
A:ASP221
|
4.9
|
36.0
|
1.0
|
CB
|
A:GLU224
|
4.9
|
29.0
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 3rv0
Go back to
Magnesium Binding Sites List in 3rv0
Magnesium binding site 2 out
of 4 in the Crystal Structure of K. Polysporus DCR1 Without the C-Terminal Dsrbd
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 K. Polysporus DCR1 Without the C-Terminal Dsrbd within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg3
b:49.9
occ:1.00
|
O
|
B:HOH390
|
2.1
|
56.5
|
1.0
|
O
|
B:HOH362
|
2.1
|
44.3
|
1.0
|
O
|
B:HOH480
|
2.2
|
54.7
|
1.0
|
OE1
|
B:GLU224
|
2.2
|
35.4
|
1.0
|
OE2
|
B:GLU147
|
2.3
|
61.0
|
1.0
|
O
|
B:HOH409
|
2.3
|
38.8
|
1.0
|
CD
|
B:GLU224
|
3.2
|
35.3
|
1.0
|
OE2
|
B:GLU224
|
3.4
|
42.4
|
1.0
|
CD
|
B:GLU147
|
3.4
|
52.0
|
1.0
|
OD1
|
B:ASP221
|
3.5
|
70.3
|
1.0
|
CG
|
B:GLU147
|
3.8
|
33.4
|
1.0
|
CE
|
B:LYS217
|
4.4
|
72.2
|
1.0
|
NZ
|
B:LYS217
|
4.5
|
70.1
|
1.0
|
OE1
|
B:GLU147
|
4.5
|
63.1
|
1.0
|
OD2
|
B:ASP151
|
4.5
|
51.6
|
1.0
|
OD1
|
B:ASN184
|
4.5
|
68.2
|
1.0
|
CG
|
B:ASP221
|
4.6
|
62.1
|
1.0
|
O
|
B:HOH472
|
4.6
|
48.0
|
1.0
|
CG
|
B:GLU224
|
4.6
|
28.3
|
1.0
|
CG
|
B:ASP151
|
4.6
|
43.8
|
1.0
|
CB
|
B:ASP151
|
4.8
|
30.1
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 3rv0
Go back to
Magnesium Binding Sites List in 3rv0
Magnesium binding site 3 out
of 4 in the Crystal Structure of K. Polysporus DCR1 Without the C-Terminal Dsrbd
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 K. Polysporus DCR1 Without the C-Terminal Dsrbd within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg4
b:40.1
occ:1.00
|
OE2
|
C:GLU147
|
2.0
|
36.7
|
1.0
|
OE1
|
C:GLU224
|
2.1
|
37.4
|
1.0
|
O
|
C:HOH370
|
2.1
|
33.7
|
1.0
|
O
|
C:HOH361
|
2.2
|
34.4
|
1.0
|
O
|
C:HOH383
|
2.2
|
28.6
|
1.0
|
CD
|
C:GLU224
|
3.1
|
41.5
|
1.0
|
CD
|
C:GLU147
|
3.2
|
42.2
|
1.0
|
OE2
|
C:GLU224
|
3.4
|
36.4
|
1.0
|
OD1
|
C:ASP221
|
3.6
|
53.1
|
1.0
|
CG
|
C:GLU147
|
3.7
|
42.6
|
1.0
|
OD2
|
C:ASP151
|
4.0
|
54.2
|
1.0
|
OD1
|
C:ASN184
|
4.1
|
53.5
|
1.0
|
OE1
|
C:GLU147
|
4.2
|
36.0
|
1.0
|
ND2
|
C:ASN184
|
4.4
|
50.7
|
1.0
|
CG
|
C:GLU224
|
4.4
|
36.3
|
1.0
|
CG
|
C:ASP221
|
4.6
|
56.5
|
1.0
|
CG
|
C:ASP151
|
4.7
|
41.5
|
1.0
|
CG
|
C:ASN184
|
4.7
|
47.6
|
1.0
|
CA
|
C:ASP221
|
4.8
|
47.6
|
1.0
|
CB
|
C:GLU224
|
4.8
|
25.4
|
1.0
|
CB
|
C:ASP151
|
4.9
|
37.0
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 3rv0
Go back to
Magnesium Binding Sites List in 3rv0
Magnesium binding site 4 out
of 4 in the Crystal Structure of K. Polysporus DCR1 Without the C-Terminal Dsrbd
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 K. Polysporus DCR1 Without the C-Terminal Dsrbd within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg2
b:56.8
occ:1.00
|
O
|
D:HOH374
|
2.2
|
61.7
|
1.0
|
O
|
D:HOH392
|
2.2
|
53.6
|
1.0
|
OE2
|
D:GLU147
|
2.2
|
76.4
|
1.0
|
O
|
D:HOH465
|
2.2
|
55.9
|
1.0
|
OE1
|
D:GLU224
|
2.3
|
50.0
|
1.0
|
OD1
|
D:ASP221
|
2.8
|
46.2
|
1.0
|
CD
|
D:GLU147
|
3.3
|
63.5
|
1.0
|
CD
|
D:GLU224
|
3.3
|
42.9
|
1.0
|
OE2
|
D:GLU224
|
3.6
|
48.2
|
1.0
|
CG
|
D:GLU147
|
3.7
|
33.2
|
1.0
|
CG
|
D:ASP221
|
3.8
|
49.4
|
1.0
|
O
|
D:HOH474
|
3.9
|
58.0
|
1.0
|
OD1
|
D:ASP151
|
4.2
|
57.5
|
1.0
|
OE1
|
D:GLU147
|
4.4
|
63.9
|
1.0
|
OD2
|
D:ASP221
|
4.5
|
54.5
|
1.0
|
CB
|
D:ASP151
|
4.6
|
32.4
|
1.0
|
CA
|
D:ASP221
|
4.6
|
44.0
|
1.0
|
CG
|
D:GLU224
|
4.7
|
35.0
|
1.0
|
CB
|
D:ASP221
|
4.7
|
35.0
|
1.0
|
CG
|
D:ASP151
|
4.7
|
50.2
|
1.0
|
|
Reference:
D.E.Weinberg,
K.Nakanishi,
D.J.Patel,
D.P.Bartel.
The Inside-Out Mechanism of Dicers From Budding Yeasts. Cell(Cambridge,Mass.) V. 146 262 2011.
ISSN: ISSN 0092-8674
PubMed: 21784247
DOI: 10.1016/J.CELL.2011.06.021
Page generated: Thu Aug 15 10:40:31 2024
|