Magnesium in PDB 5xhi: Crystal Structure of Frog M-Ferritin D38A Mutant
Enzymatic activity of Crystal Structure of Frog M-Ferritin D38A Mutant
All present enzymatic activity of Crystal Structure of Frog M-Ferritin D38A Mutant:
1.16.3.1;
Protein crystallography data
The structure of Crystal Structure of Frog M-Ferritin D38A Mutant, PDB code: 5xhi
was solved by
M.K.Jagdev,
D.Vasudevan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
31.12 /
1.26
|
Space group
|
F 4 3 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
184.090,
184.090,
184.090,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
12.5 /
15.3
|
Other elements in 5xhi:
The structure of Crystal Structure of Frog M-Ferritin D38A Mutant also contains other interesting chemical elements:
Magnesium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
11;
Binding sites:
The binding sites of Magnesium atom in the Crystal Structure of Frog M-Ferritin D38A Mutant
(pdb code 5xhi). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 11 binding sites of Magnesium where determined in the
Crystal Structure of Frog M-Ferritin D38A Mutant, PDB code: 5xhi:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Magnesium binding site 1 out
of 11 in 5xhi
Go back to
Magnesium Binding Sites List in 5xhi
Magnesium binding site 1 out
of 11 in the Crystal Structure of Frog M-Ferritin D38A Mutant
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 Frog M-Ferritin D38A Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg201
b:11.3
occ:0.75
|
OE2
|
A:GLU57
|
2.0
|
11.9
|
0.8
|
OE1
|
A:GLU136
|
2.0
|
7.5
|
0.5
|
O
|
A:HOH423
|
2.0
|
16.6
|
1.0
|
OD2
|
A:ASP140
|
2.1
|
13.8
|
1.0
|
O
|
A:HOH327
|
2.1
|
16.9
|
1.0
|
O
|
A:HOH395
|
2.1
|
13.8
|
1.0
|
CG
|
A:ASP140
|
3.0
|
11.2
|
1.0
|
CD
|
A:GLU57
|
3.0
|
10.5
|
0.5
|
CD
|
A:GLU136
|
3.3
|
8.0
|
0.5
|
OD1
|
A:ASP140
|
3.3
|
15.9
|
1.0
|
OE1
|
A:GLU57
|
3.4
|
9.5
|
0.5
|
O
|
A:GLU136
|
3.8
|
10.0
|
1.0
|
CB
|
A:GLU136
|
3.9
|
12.7
|
1.0
|
O
|
A:HOH317
|
3.9
|
15.7
|
1.0
|
O
|
A:HOH383
|
4.0
|
15.3
|
1.0
|
CG
|
A:GLU136
|
4.1
|
13.5
|
1.0
|
O
|
A:HOH523
|
4.2
|
38.9
|
1.0
|
OE2
|
A:GLU136
|
4.2
|
7.8
|
0.5
|
C
|
A:GLU136
|
4.3
|
9.5
|
1.0
|
CG
|
A:GLU57
|
4.3
|
12.7
|
1.0
|
CB
|
A:ASP140
|
4.4
|
10.3
|
1.0
|
CA
|
A:GLU136
|
4.5
|
10.8
|
1.0
|
O
|
A:HOH482
|
4.5
|
37.1
|
1.0
|
O
|
A:HOH462
|
4.6
|
34.0
|
1.0
|
CE1
|
A:HIS61
|
4.8
|
34.1
|
1.0
|
MG
|
A:MG209
|
4.8
|
6.5
|
0.5
|
O
|
A:HOH348
|
4.9
|
19.0
|
1.0
|
|
Magnesium binding site 2 out
of 11 in 5xhi
Go back to
Magnesium Binding Sites List in 5xhi
Magnesium binding site 2 out
of 11 in the Crystal Structure of Frog M-Ferritin D38A Mutant
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 Frog M-Ferritin D38A Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg202
b:13.4
occ:0.75
|
O
|
A:HOH507
|
2.0
|
23.6
|
1.0
|
O
|
A:HOH351
|
2.0
|
15.4
|
1.0
|
O
|
A:HOH428
|
2.0
|
20.6
|
1.0
|
O
|
A:HOH430
|
2.1
|
21.9
|
1.0
|
OG
|
A:SER10
|
2.1
|
12.5
|
1.0
|
O
|
A:HOH406
|
2.1
|
12.2
|
1.0
|
CB
|
A:SER10
|
3.2
|
10.6
|
1.0
|
CA
|
A:SER10
|
3.9
|
8.2
|
1.0
|
O
|
A:SER10
|
4.1
|
8.0
|
1.0
|
OE1
|
A:GLU13
|
4.2
|
9.6
|
1.0
|
O
|
A:HOH483
|
4.3
|
33.3
|
1.0
|
O
|
A:HOH336
|
4.3
|
16.5
|
1.0
|
O
|
A:HOH487
|
4.3
|
32.7
|
1.0
|
C
|
A:SER10
|
4.4
|
7.3
|
1.0
|
O
|
A:HOH475
|
4.4
|
14.0
|
1.0
|
O
|
A:HOH561
|
4.6
|
37.9
|
1.0
|
CD
|
A:GLU13
|
4.7
|
7.0
|
1.0
|
|
Magnesium binding site 3 out
of 11 in 5xhi
Go back to
Magnesium Binding Sites List in 5xhi
Magnesium binding site 3 out
of 11 in the Crystal Structure of Frog M-Ferritin D38A Mutant
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 Frog M-Ferritin D38A Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg203
b:10.6
occ:0.75
|
O
|
A:HOH344
|
2.0
|
17.5
|
1.0
|
OD2
|
A:ASP127
|
4.0
|
13.2
|
1.0
|
O
|
A:HOH533
|
4.2
|
27.9
|
1.0
|
OD1
|
A:ASP127
|
4.4
|
13.3
|
1.0
|
O
|
A:HOH484
|
4.4
|
66.7
|
1.0
|
CG
|
A:ASP127
|
4.6
|
11.8
|
1.0
|
O
|
A:HOH369
|
4.7
|
26.3
|
1.0
|
OG
|
A:SER131
|
4.7
|
13.5
|
0.7
|
O
|
A:HOH519
|
4.8
|
31.6
|
1.0
|
OG
|
A:SER131
|
4.9
|
14.3
|
0.3
|
|
Magnesium binding site 4 out
of 11 in 5xhi
Go back to
Magnesium Binding Sites List in 5xhi
Magnesium binding site 4 out
of 11 in the Crystal Structure of Frog M-Ferritin D38A Mutant
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 Frog M-Ferritin D38A Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg204
b:6.4
occ:0.25
|
O
|
A:HOH563
|
2.1
|
10.7
|
1.0
|
O
|
A:HOH339
|
2.1
|
9.5
|
1.0
|
OE2
|
A:GLU130
|
3.9
|
10.1
|
1.0
|
OE1
|
A:GLU130
|
4.3
|
14.7
|
1.0
|
O
|
A:HOH510
|
4.3
|
10.8
|
1.0
|
O
|
A:HOH567
|
4.3
|
14.0
|
1.0
|
CD
|
A:GLU130
|
4.5
|
11.1
|
1.0
|
|
Magnesium binding site 5 out
of 11 in 5xhi
Go back to
Magnesium Binding Sites List in 5xhi
Magnesium binding site 5 out
of 11 in the Crystal Structure of Frog M-Ferritin D38A Mutant
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Crystal Structure of Frog M-Ferritin D38A Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg205
b:17.3
occ:0.70
|
O
|
A:HOH546
|
1.8
|
23.6
|
1.0
|
O
|
A:HOH566
|
1.9
|
29.4
|
1.0
|
O
|
A:HOH505
|
2.1
|
16.0
|
1.0
|
O
|
A:HOH557
|
2.1
|
26.8
|
1.0
|
O
|
A:HOH410
|
2.1
|
32.6
|
1.0
|
O
|
A:HOH508
|
2.5
|
35.7
|
1.0
|
O
|
A:HOH441
|
3.9
|
9.8
|
1.0
|
O
|
A:HOH503
|
4.4
|
29.6
|
1.0
|
O
|
A:VAL1
|
4.7
|
18.9
|
1.0
|
|
Magnesium binding site 6 out
of 11 in 5xhi
Go back to
Magnesium Binding Sites List in 5xhi
Magnesium binding site 6 out
of 11 in the Crystal Structure of Frog M-Ferritin D38A Mutant
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Crystal Structure of Frog M-Ferritin D38A Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg206
b:11.5
occ:0.25
|
O
|
A:HOH343
|
1.8
|
28.5
|
1.0
|
O
|
A:HOH310
|
2.1
|
31.8
|
1.0
|
OD1
|
A:ASP127
|
3.8
|
13.3
|
1.0
|
OG
|
A:SER131
|
4.1
|
13.5
|
0.7
|
OE1
|
A:GLU130
|
4.2
|
14.7
|
1.0
|
O
|
A:HOH369
|
4.2
|
26.3
|
1.0
|
CB
|
A:GLU130
|
4.8
|
9.1
|
1.0
|
CG
|
A:ASP127
|
4.9
|
11.8
|
1.0
|
O
|
A:HOH490
|
4.9
|
14.9
|
1.0
|
CD
|
A:GLU130
|
5.0
|
11.1
|
1.0
|
|
Magnesium binding site 7 out
of 11 in 5xhi
Go back to
Magnesium Binding Sites List in 5xhi
Magnesium binding site 7 out
of 11 in the Crystal Structure of Frog M-Ferritin D38A Mutant
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Crystal Structure of Frog M-Ferritin D38A Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg207
b:6.9
occ:0.35
|
CD
|
A:LYS82
|
4.3
|
9.8
|
0.3
|
O
|
A:HOH558
|
4.4
|
16.0
|
1.0
|
CE
|
A:LYS83
|
4.5
|
10.2
|
0.7
|
CE
|
A:LYS82
|
4.6
|
8.3
|
0.3
|
NZ
|
A:LYS82
|
4.8
|
15.7
|
0.7
|
CE
|
A:LYS83
|
4.8
|
5.5
|
0.3
|
O
|
A:HOH456
|
4.9
|
58.6
|
1.0
|
CD
|
A:LYS82
|
4.9
|
10.4
|
0.7
|
|
Magnesium binding site 8 out
of 11 in 5xhi
Go back to
Magnesium Binding Sites List in 5xhi
Magnesium binding site 8 out
of 11 in the Crystal Structure of Frog M-Ferritin D38A Mutant
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Crystal Structure of Frog M-Ferritin D38A Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg208
b:13.9
occ:0.15
|
O
|
A:HOH538
|
2.9
|
15.0
|
1.0
|
O
|
A:HOH567
|
4.2
|
14.0
|
1.0
|
CG2
|
A:THR118
|
4.4
|
11.0
|
1.0
|
O
|
A:HOH539
|
4.7
|
17.6
|
1.0
|
CL
|
A:CL230
|
4.8
|
18.4
|
0.7
|
|
Magnesium binding site 9 out
of 11 in 5xhi
Go back to
Magnesium Binding Sites List in 5xhi
Magnesium binding site 9 out
of 11 in the Crystal Structure of Frog M-Ferritin D38A Mutant
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 9 of Crystal Structure of Frog M-Ferritin D38A Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg209
b:6.5
occ:0.50
|
O
|
A:HOH317
|
2.0
|
15.7
|
1.0
|
OE1
|
A:GLN137
|
2.0
|
12.6
|
0.9
|
OE2
|
A:GLU136
|
2.0
|
7.8
|
0.5
|
O
|
A:HOH389
|
2.1
|
15.3
|
1.0
|
O
|
A:HOH383
|
2.1
|
15.3
|
1.0
|
O
|
A:HOH332
|
2.2
|
14.5
|
1.0
|
CD
|
A:GLU136
|
3.0
|
8.0
|
0.5
|
CD
|
A:GLN137
|
3.0
|
12.2
|
1.0
|
OE1
|
A:GLU136
|
3.3
|
7.5
|
0.5
|
NE2
|
A:GLN137
|
3.6
|
12.5
|
1.0
|
ND1
|
A:HIS61
|
3.9
|
26.9
|
1.0
|
OE1
|
A:GLU103
|
4.0
|
12.2
|
1.0
|
CE1
|
A:HIS61
|
4.0
|
34.1
|
1.0
|
OE1
|
A:GLU58
|
4.0
|
13.2
|
1.0
|
OE2
|
A:GLU58
|
4.0
|
17.4
|
1.0
|
CA
|
A:GLN137
|
4.2
|
7.8
|
1.0
|
CG
|
A:GLN137
|
4.2
|
11.0
|
1.0
|
OD2
|
A:ASP140
|
4.3
|
13.8
|
1.0
|
CB
|
A:GLN137
|
4.3
|
11.2
|
1.0
|
CG
|
A:GLU136
|
4.4
|
13.5
|
1.0
|
OE2
|
A:GLU57
|
4.5
|
11.9
|
0.8
|
CD
|
A:GLU58
|
4.5
|
12.5
|
1.0
|
N
|
A:GLN137
|
4.5
|
9.1
|
1.0
|
OE2
|
A:GLU23
|
4.6
|
13.6
|
1.0
|
O
|
A:HOH348
|
4.8
|
19.0
|
1.0
|
MG
|
A:MG201
|
4.8
|
11.3
|
0.8
|
CG1
|
A:VAL106
|
4.9
|
9.1
|
1.0
|
C
|
A:GLU136
|
4.9
|
9.5
|
1.0
|
|
Magnesium binding site 10 out
of 11 in 5xhi
Go back to
Magnesium Binding Sites List in 5xhi
Magnesium binding site 10 out
of 11 in the Crystal Structure of Frog M-Ferritin D38A Mutant
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 10 of Crystal Structure of Frog M-Ferritin D38A Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg210
b:0.7
occ:0.25
|
NE2
|
A:HIS169
|
3.2
|
10.2
|
1.0
|
CE1
|
A:HIS169
|
3.9
|
12.1
|
1.0
|
CD2
|
A:LEU165
|
3.9
|
11.9
|
1.0
|
CD2
|
A:HIS169
|
4.3
|
8.2
|
1.0
|
MG
|
A:MG211
|
4.9
|
0.0
|
0.3
|
|
Reference:
B.Subhadarshanee,
A.Mohanty,
M.K.Jagdev,
D.Vasudevan,
R.K.Behera.
Surface Charge Dependent Separation of Modified and Hybrid Ferritin in Native Page: Impact of Lysine 104 Biochim. Biophys. Acta V.1865 1267 2017.
ISSN: ISSN 0006-3002
PubMed: 28739445
DOI: 10.1016/J.BBAPAP.2017.07.012
Page generated: Mon Sep 30 09:22:21 2024
|