Magnesium in PDB 3i6b: Crystal Structure of Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate
Enzymatic activity of Crystal Structure of Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate
All present enzymatic activity of Crystal Structure of Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate:
3.1.3.45;
Protein crystallography data
The structure of Crystal Structure of Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate, PDB code: 3i6b
was solved by
T.Biswas,
O.V.Tsodikov,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
40.00 /
2.49
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
64.964,
144.104,
145.854,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20 /
23.8
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate
(pdb code 3i6b). 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 Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate, PDB code: 3i6b:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 3i6b
Go back to
Magnesium Binding Sites List in 3i6b
Magnesium binding site 1 out
of 4 in the Crystal Structure of Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate
 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 Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg201
b:49.5
occ:1.00
|
O1
|
A:PO4800
|
2.3
|
75.7
|
1.0
|
O
|
A:ASP34
|
2.4
|
25.4
|
1.0
|
O
|
A:HOH699
|
2.6
|
34.1
|
1.0
|
OD2
|
A:ASP125
|
2.9
|
26.9
|
1.0
|
C
|
A:ASP34
|
3.6
|
25.4
|
1.0
|
OD2
|
A:ASP32
|
3.8
|
30.4
|
1.0
|
P
|
A:PO4800
|
3.8
|
75.3
|
1.0
|
CG
|
A:ASP125
|
3.9
|
26.1
|
1.0
|
CG1
|
B:VAL56
|
4.1
|
23.8
|
1.0
|
CB
|
A:ASP34
|
4.1
|
25.9
|
1.0
|
CB
|
A:ASP125
|
4.2
|
23.6
|
1.0
|
CA
|
A:ASP34
|
4.3
|
25.6
|
1.0
|
O2
|
A:PO4800
|
4.4
|
75.3
|
1.0
|
CB
|
A:ASP126
|
4.6
|
22.4
|
1.0
|
N
|
A:ASP34
|
4.6
|
25.3
|
1.0
|
CG
|
A:ASP32
|
4.6
|
27.9
|
1.0
|
O4
|
A:PO4800
|
4.6
|
75.8
|
1.0
|
N
|
A:GLY35
|
4.6
|
25.2
|
1.0
|
O3
|
A:PO4800
|
4.6
|
75.3
|
1.0
|
OD2
|
A:ASP129
|
4.8
|
23.2
|
1.0
|
CB
|
A:ASP32
|
4.8
|
25.8
|
1.0
|
N
|
A:ASP126
|
4.8
|
22.4
|
1.0
|
CA
|
A:GLY35
|
4.8
|
25.1
|
1.0
|
O8
|
B:KDO900
|
4.9
|
77.3
|
1.0
|
CA
|
A:ASP125
|
5.0
|
23.1
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 3i6b
Go back to
Magnesium Binding Sites List in 3i6b
Magnesium binding site 2 out
of 4 in the Crystal Structure of Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate
 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 Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg202
b:55.6
occ:1.00
|
O1
|
B:PO4800
|
2.6
|
33.1
|
1.0
|
OD2
|
B:ASP32
|
2.7
|
28.6
|
1.0
|
O
|
B:ASP34
|
2.7
|
23.1
|
1.0
|
OD2
|
B:ASP125
|
2.8
|
29.0
|
1.0
|
CG
|
B:ASP32
|
3.3
|
25.9
|
1.0
|
O4
|
B:PO4800
|
3.4
|
31.3
|
1.0
|
P
|
B:PO4800
|
3.5
|
33.4
|
1.0
|
CB
|
B:ASP32
|
3.6
|
24.3
|
1.0
|
C
|
B:ASP34
|
3.7
|
23.2
|
1.0
|
CG
|
B:ASP125
|
3.9
|
26.2
|
1.0
|
O2
|
B:PO4800
|
3.9
|
30.4
|
1.0
|
N
|
B:ASP34
|
4.0
|
23.5
|
1.0
|
CB
|
B:ASP34
|
4.0
|
23.4
|
1.0
|
CA
|
B:ASP34
|
4.1
|
23.3
|
1.0
|
OD1
|
B:ASP32
|
4.1
|
27.6
|
1.0
|
OD2
|
B:ASP129
|
4.1
|
26.0
|
1.0
|
O
|
B:HOH701
|
4.2
|
34.9
|
1.0
|
OD1
|
B:ASP129
|
4.6
|
25.8
|
1.0
|
OD1
|
B:ASP125
|
4.6
|
28.8
|
1.0
|
CA
|
B:ASP32
|
4.7
|
23.8
|
1.0
|
N
|
B:VAL33
|
4.8
|
23.5
|
1.0
|
CG
|
B:ASP129
|
4.8
|
25.0
|
1.0
|
O3
|
B:PO4800
|
4.8
|
31.1
|
1.0
|
C
|
B:VAL33
|
4.9
|
23.6
|
1.0
|
CB
|
B:ASP125
|
4.9
|
24.0
|
1.0
|
N
|
B:ASP125
|
4.9
|
22.8
|
1.0
|
N
|
B:GLY35
|
4.9
|
23.0
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 3i6b
Go back to
Magnesium Binding Sites List in 3i6b
Magnesium binding site 3 out
of 4 in the Crystal Structure of Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate
 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 Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg204
b:32.5
occ:1.00
|
O3
|
C:PO4800
|
2.2
|
60.3
|
1.0
|
OD1
|
C:ASP125
|
2.2
|
32.3
|
1.0
|
O
|
C:ASP34
|
2.5
|
24.9
|
1.0
|
CG
|
C:ASP125
|
3.2
|
29.0
|
1.0
|
OD2
|
C:ASP32
|
3.2
|
27.5
|
1.0
|
OD2
|
C:ASP125
|
3.5
|
31.9
|
1.0
|
P
|
C:PO4800
|
3.6
|
60.1
|
1.0
|
C
|
C:ASP34
|
3.7
|
25.1
|
1.0
|
O2
|
C:PO4800
|
4.0
|
59.7
|
1.0
|
CG
|
C:ASP32
|
4.0
|
25.8
|
1.0
|
O
|
C:HOH549
|
4.0
|
28.2
|
1.0
|
CB
|
C:ASP32
|
4.3
|
23.7
|
1.0
|
O4
|
C:PO4800
|
4.3
|
60.7
|
1.0
|
CG1
|
D:VAL56
|
4.4
|
24.8
|
1.0
|
CB
|
C:ASP34
|
4.4
|
25.5
|
1.0
|
CA
|
C:ASP34
|
4.4
|
25.2
|
1.0
|
CB
|
C:ASP126
|
4.5
|
25.8
|
1.0
|
OD2
|
C:ASP129
|
4.5
|
27.5
|
1.0
|
CB
|
C:ASP125
|
4.5
|
26.3
|
1.0
|
O1
|
C:PO4800
|
4.6
|
60.7
|
1.0
|
N
|
C:GLY35
|
4.7
|
24.9
|
1.0
|
N
|
C:ASP34
|
4.7
|
24.8
|
1.0
|
N
|
C:ASP126
|
4.7
|
25.6
|
1.0
|
CA
|
C:GLY35
|
4.8
|
24.7
|
1.0
|
N
|
C:ASP125
|
4.9
|
25.0
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 3i6b
Go back to
Magnesium Binding Sites List in 3i6b
Magnesium binding site 4 out
of 4 in the Crystal Structure of Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate
 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 Yrbi Lacking the Last 8 Residues, in Complex with Kdo and Inorganic Phosphate within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg203
b:49.2
occ:1.00
|
O2
|
D:PO4800
|
2.2
|
33.1
|
1.0
|
OD2
|
D:ASP125
|
2.9
|
28.8
|
1.0
|
O
|
D:ASP34
|
3.4
|
24.4
|
1.0
|
P
|
D:PO4800
|
3.5
|
33.7
|
1.0
|
OD2
|
D:ASP32
|
3.5
|
28.6
|
1.0
|
OD2
|
D:ASP129
|
3.6
|
27.9
|
1.0
|
O1
|
D:PO4800
|
3.8
|
33.0
|
1.0
|
CD1
|
D:ILE128
|
3.8
|
30.6
|
1.0
|
CG
|
D:ASP32
|
3.9
|
26.8
|
1.0
|
O
|
D:HOH677
|
3.9
|
31.5
|
1.0
|
OD1
|
D:ASP129
|
4.0
|
28.5
|
1.0
|
CB
|
D:ASP32
|
4.1
|
24.8
|
1.0
|
CG
|
D:ASP125
|
4.2
|
27.1
|
1.0
|
CG
|
D:ASP129
|
4.2
|
26.9
|
1.0
|
O4
|
D:PO4800
|
4.3
|
32.3
|
1.0
|
C
|
D:ASP34
|
4.5
|
24.1
|
1.0
|
O3
|
D:PO4800
|
4.5
|
32.1
|
1.0
|
OD1
|
D:ASP32
|
4.6
|
29.8
|
1.0
|
CG1
|
D:ILE128
|
4.7
|
28.1
|
1.0
|
CB
|
D:ASP34
|
4.7
|
24.1
|
1.0
|
CB
|
D:ASP126
|
4.8
|
24.9
|
1.0
|
N
|
D:ASP126
|
4.8
|
25.1
|
1.0
|
N
|
D:ASP125
|
4.9
|
24.8
|
1.0
|
OD1
|
D:ASP125
|
4.9
|
29.1
|
1.0
|
CA
|
D:ASP34
|
5.0
|
24.1
|
1.0
|
|
Reference:
T.Biswas,
L.Yi,
P.Aggarwal,
J.Wu,
J.R.Rubin,
J.A.Stuckey,
R.W.Woodard,
O.V.Tsodikov.
The Tail of Kdsc: Conformational Changes Control the Activity of A Haloacid Dehalogenase Superfamily Phosphatase. J.Biol.Chem. V. 284 30594 2009.
ISSN: ISSN 0021-9258
PubMed: 19726684
DOI: 10.1074/JBC.M109.012278
Page generated: Wed Aug 14 15:58:15 2024
|