Magnesium in PDB 7ebe: Crystal Structure of Isocitrate Lyase-1 From Candida Albicans
Enzymatic activity of Crystal Structure of Isocitrate Lyase-1 From Candida Albicans
All present enzymatic activity of Crystal Structure of Isocitrate Lyase-1 From Candida Albicans:
4.1.3.1;
Protein crystallography data
The structure of Crystal Structure of Isocitrate Lyase-1 From Candida Albicans, PDB code: 7ebe
was solved by
K.Hiragi,
K.Nishio,
S.Moriyama,
T.Hamaguchi,
A.Mizoguchi,
K.Yonekura,
K.Tani,
T.Mizushima,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.11 /
2.69
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
80.971,
139.91,
200.301,
90,
92.55,
90
|
R / Rfree (%)
|
21.5 /
24.8
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Isocitrate Lyase-1 From Candida Albicans
(pdb code 7ebe). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the
Crystal Structure of Isocitrate Lyase-1 From Candida Albicans, PDB code: 7ebe:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 7ebe
Go back to
Magnesium Binding Sites List in 7ebe
Magnesium binding site 1 out
of 8 in the Crystal Structure of Isocitrate Lyase-1 From Candida Albicans
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 Isocitrate Lyase-1 From Candida Albicans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg601
b:46.5
occ:1.00
|
O
|
A:HOH707
|
2.1
|
48.4
|
1.0
|
O
|
A:HOH702
|
2.2
|
44.1
|
1.0
|
O
|
A:HOH709
|
2.6
|
42.3
|
1.0
|
OD2
|
A:ASP172
|
2.7
|
47.1
|
1.0
|
O
|
A:HOH705
|
2.8
|
42.1
|
1.0
|
N
|
A:TRP103
|
2.9
|
65.9
|
1.0
|
N
|
A:GLY102
|
3.3
|
56.4
|
1.0
|
OG
|
A:SER101
|
3.5
|
59.0
|
1.0
|
OD2
|
A:ASP118
|
3.5
|
69.0
|
1.0
|
CB
|
A:TRP103
|
3.5
|
65.2
|
1.0
|
O
|
A:HOH701
|
3.6
|
46.2
|
1.0
|
CA
|
A:GLY102
|
3.7
|
55.1
|
1.0
|
C
|
A:GLY102
|
3.7
|
59.0
|
1.0
|
CA
|
A:TRP103
|
3.8
|
63.5
|
1.0
|
C
|
A:FMT602
|
3.8
|
72.3
|
1.0
|
O1
|
A:FMT602
|
3.8
|
76.8
|
1.0
|
CG
|
A:ASP172
|
3.9
|
48.6
|
1.0
|
OH
|
A:TYR99
|
4.0
|
51.4
|
1.0
|
CG
|
A:ASP118
|
4.2
|
72.9
|
1.0
|
C
|
A:SER101
|
4.2
|
52.5
|
1.0
|
OD1
|
A:ASP118
|
4.3
|
72.4
|
1.0
|
CA
|
A:SER101
|
4.5
|
52.4
|
1.0
|
CB
|
A:SER101
|
4.5
|
57.0
|
1.0
|
CB
|
A:ASP172
|
4.6
|
45.4
|
1.0
|
O2
|
A:FMT602
|
4.8
|
70.1
|
1.0
|
CG
|
A:TRP103
|
4.8
|
64.8
|
1.0
|
OD1
|
A:ASP172
|
4.9
|
45.2
|
1.0
|
O
|
A:GLY102
|
4.9
|
61.4
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 7ebe
Go back to
Magnesium Binding Sites List in 7ebe
Magnesium binding site 2 out
of 8 in the Crystal Structure of Isocitrate Lyase-1 From Candida Albicans
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 Isocitrate Lyase-1 From Candida Albicans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg601
b:63.1
occ:1.00
|
O
|
B:HOH706
|
1.9
|
60.1
|
1.0
|
OD2
|
B:ASP172
|
2.0
|
55.5
|
1.0
|
O
|
B:HOH701
|
2.3
|
52.0
|
1.0
|
O
|
B:HOH715
|
2.9
|
38.5
|
1.0
|
CG
|
B:ASP172
|
3.2
|
53.3
|
1.0
|
O1
|
B:FMT602
|
3.3
|
84.5
|
1.0
|
N
|
B:TRP103
|
3.4
|
58.9
|
1.0
|
OD2
|
B:ASP118
|
3.4
|
92.6
|
1.0
|
N
|
B:GLY102
|
3.6
|
56.6
|
1.0
|
CA
|
B:GLY102
|
3.7
|
61.6
|
1.0
|
OD1
|
B:ASP118
|
3.9
|
79.6
|
1.0
|
C
|
B:GLY102
|
3.9
|
59.0
|
1.0
|
OD1
|
B:ASP172
|
3.9
|
55.1
|
1.0
|
CG
|
B:ASP118
|
4.0
|
77.2
|
1.0
|
NZ
|
B:LYS208
|
4.1
|
75.8
|
1.0
|
C
|
B:FMT602
|
4.1
|
83.6
|
1.0
|
OD1
|
B:ASP174
|
4.1
|
59.1
|
1.0
|
CB
|
B:ASP172
|
4.2
|
52.1
|
1.0
|
O2
|
B:FMT602
|
4.3
|
78.1
|
1.0
|
CA
|
B:TRP103
|
4.4
|
59.9
|
1.0
|
CB
|
B:TRP103
|
4.4
|
60.1
|
1.0
|
OH
|
B:TYR99
|
4.4
|
55.3
|
1.0
|
OG
|
B:SER101
|
4.6
|
59.3
|
1.0
|
OE1
|
B:GLU201
|
4.8
|
66.5
|
1.0
|
C
|
B:SER101
|
4.8
|
55.6
|
1.0
|
CE
|
B:LYS208
|
4.8
|
76.4
|
1.0
|
CE1
|
B:HIS199
|
4.9
|
49.5
|
1.0
|
O
|
B:GLY102
|
5.0
|
57.7
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 7ebe
Go back to
Magnesium Binding Sites List in 7ebe
Magnesium binding site 3 out
of 8 in the Crystal Structure of Isocitrate Lyase-1 From Candida Albicans
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 Isocitrate Lyase-1 From Candida Albicans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg601
b:52.8
occ:1.00
|
O
|
C:HOH707
|
1.9
|
44.3
|
1.0
|
OD2
|
C:ASP172
|
2.3
|
48.9
|
1.0
|
O
|
C:HOH718
|
2.3
|
46.3
|
1.0
|
O
|
C:HOH704
|
2.5
|
43.7
|
1.0
|
O
|
C:HOH702
|
2.8
|
44.0
|
1.0
|
O
|
C:HOH701
|
2.9
|
46.9
|
1.0
|
N
|
C:TRP103
|
3.2
|
60.5
|
1.0
|
N
|
C:GLY102
|
3.4
|
59.2
|
1.0
|
CG
|
C:ASP172
|
3.5
|
51.1
|
1.0
|
OD2
|
C:ASP118
|
3.6
|
61.6
|
1.0
|
CA
|
C:GLY102
|
3.7
|
56.9
|
1.0
|
O2
|
C:FMT602
|
3.8
|
70.0
|
1.0
|
C
|
C:GLY102
|
3.9
|
59.2
|
1.0
|
OG
|
C:SER101
|
4.0
|
60.2
|
1.0
|
OH
|
C:TYR99
|
4.0
|
53.3
|
1.0
|
CB
|
C:TRP103
|
4.0
|
64.7
|
1.0
|
C
|
C:FMT602
|
4.1
|
68.0
|
1.0
|
CA
|
C:TRP103
|
4.1
|
59.1
|
1.0
|
OD1
|
C:ASP118
|
4.2
|
59.4
|
1.0
|
CG
|
C:ASP118
|
4.3
|
61.7
|
1.0
|
CB
|
C:ASP172
|
4.3
|
48.6
|
1.0
|
OD1
|
C:ASP172
|
4.4
|
54.2
|
1.0
|
C
|
C:SER101
|
4.4
|
54.5
|
1.0
|
CA
|
C:SER101
|
4.7
|
51.6
|
1.0
|
NZ
|
C:LYS208
|
4.8
|
73.4
|
1.0
|
OD1
|
C:ASP174
|
4.9
|
56.0
|
1.0
|
CB
|
C:SER101
|
4.9
|
55.6
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 7ebe
Go back to
Magnesium Binding Sites List in 7ebe
Magnesium binding site 4 out
of 8 in the Crystal Structure of Isocitrate Lyase-1 From Candida Albicans
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 Isocitrate Lyase-1 From Candida Albicans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg601
b:66.4
occ:1.00
|
O
|
D:HOH703
|
1.9
|
65.1
|
1.0
|
O
|
D:HOH705
|
2.4
|
48.8
|
1.0
|
OD2
|
D:ASP172
|
2.5
|
60.2
|
1.0
|
O
|
D:HOH709
|
2.5
|
45.9
|
1.0
|
O1
|
D:FMT602
|
3.0
|
72.5
|
1.0
|
OD2
|
D:ASP118
|
3.3
|
70.7
|
1.0
|
N
|
D:TRP103
|
3.3
|
64.9
|
1.0
|
CG
|
D:ASP172
|
3.7
|
50.9
|
1.0
|
N
|
D:GLY102
|
3.7
|
52.7
|
1.0
|
CA
|
D:GLY102
|
3.9
|
54.3
|
1.0
|
CB
|
D:TRP103
|
4.0
|
66.3
|
1.0
|
C
|
D:GLY102
|
4.0
|
57.2
|
1.0
|
CG
|
D:ASP118
|
4.0
|
67.5
|
1.0
|
OD1
|
D:ASP118
|
4.0
|
73.4
|
1.0
|
C
|
D:FMT602
|
4.1
|
63.1
|
1.0
|
CA
|
D:TRP103
|
4.1
|
61.0
|
1.0
|
OG
|
D:SER101
|
4.2
|
51.6
|
1.0
|
OH
|
D:TYR99
|
4.3
|
50.5
|
1.0
|
NZ
|
D:LYS208
|
4.5
|
82.6
|
1.0
|
OD1
|
D:ASP172
|
4.5
|
53.8
|
1.0
|
O2
|
D:FMT602
|
4.5
|
63.5
|
1.0
|
CB
|
D:ASP172
|
4.6
|
51.3
|
1.0
|
C
|
D:SER101
|
4.7
|
48.8
|
1.0
|
OD1
|
D:ASP174
|
4.8
|
52.8
|
1.0
|
NH1
|
D:ARG247
|
5.0
|
55.5
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 7ebe
Go back to
Magnesium Binding Sites List in 7ebe
Magnesium binding site 5 out
of 8 in the Crystal Structure of Isocitrate Lyase-1 From Candida Albicans
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 Isocitrate Lyase-1 From Candida Albicans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg601
b:69.9
occ:1.00
|
O
|
E:HOH702
|
1.7
|
74.5
|
1.0
|
OD2
|
E:ASP172
|
2.2
|
67.4
|
1.0
|
O
|
E:HOH714
|
2.6
|
54.8
|
1.0
|
OD2
|
E:ASP118
|
3.2
|
95.2
|
1.0
|
CG
|
E:ASP172
|
3.4
|
67.0
|
1.0
|
N
|
E:TRP103
|
3.6
|
73.6
|
1.0
|
OD1
|
E:ASP118
|
3.9
|
81.9
|
1.0
|
N
|
E:GLY102
|
3.9
|
76.1
|
1.0
|
CG
|
E:ASP118
|
4.0
|
84.2
|
1.0
|
NZ
|
E:LYS208
|
4.0
|
88.6
|
1.0
|
CA
|
E:GLY102
|
4.0
|
77.0
|
1.0
|
OD1
|
E:ASP172
|
4.1
|
66.7
|
1.0
|
C
|
E:GLY102
|
4.2
|
72.9
|
1.0
|
OD1
|
E:ASP174
|
4.3
|
60.6
|
1.0
|
CB
|
E:ASP172
|
4.5
|
61.5
|
1.0
|
OH
|
E:TYR99
|
4.5
|
78.8
|
1.0
|
CA
|
E:TRP103
|
4.5
|
78.1
|
1.0
|
OE2
|
E:GLU201
|
4.6
|
82.0
|
1.0
|
CB
|
E:TRP103
|
4.6
|
79.9
|
1.0
|
NH1
|
E:ARG247
|
4.7
|
77.4
|
1.0
|
OG
|
E:SER101
|
4.8
|
72.9
|
1.0
|
CE
|
E:LYS208
|
4.8
|
86.4
|
1.0
|
CE1
|
E:HIS199
|
4.9
|
61.1
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 7ebe
Go back to
Magnesium Binding Sites List in 7ebe
Magnesium binding site 6 out
of 8 in the Crystal Structure of Isocitrate Lyase-1 From Candida Albicans
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 Isocitrate Lyase-1 From Candida Albicans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg601
b:71.1
occ:1.00
|
O
|
F:HOH706
|
2.0
|
81.2
|
1.0
|
OD2
|
F:ASP172
|
2.1
|
70.3
|
1.0
|
O
|
F:HOH711
|
2.1
|
50.0
|
1.0
|
CG
|
F:ASP172
|
3.3
|
67.3
|
1.0
|
OD2
|
F:ASP118
|
3.6
|
79.2
|
1.0
|
N
|
F:TRP103
|
3.8
|
76.8
|
1.0
|
N
|
F:GLY102
|
3.9
|
71.2
|
1.0
|
OD1
|
F:ASP172
|
4.0
|
68.7
|
1.0
|
OH
|
F:TYR99
|
4.1
|
63.7
|
1.0
|
CA
|
F:GLY102
|
4.1
|
71.9
|
1.0
|
NZ
|
F:LYS208
|
4.3
|
91.6
|
1.0
|
OD1
|
F:ASP118
|
4.3
|
95.6
|
1.0
|
CG
|
F:ASP118
|
4.3
|
86.0
|
1.0
|
CB
|
F:ASP172
|
4.3
|
64.5
|
1.0
|
C
|
F:GLY102
|
4.4
|
70.7
|
1.0
|
OE2
|
F:GLU201
|
4.5
|
92.9
|
1.0
|
CB
|
F:TRP103
|
4.6
|
76.5
|
1.0
|
NH1
|
F:ARG247
|
4.6
|
70.6
|
1.0
|
OD1
|
F:ASP174
|
4.6
|
65.6
|
1.0
|
OG
|
F:SER101
|
4.6
|
66.7
|
1.0
|
CE1
|
F:HIS199
|
4.7
|
56.9
|
1.0
|
CA
|
F:TRP103
|
4.7
|
71.0
|
1.0
|
NE2
|
F:HIS199
|
4.9
|
52.9
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 7ebe
Go back to
Magnesium Binding Sites List in 7ebe
Magnesium binding site 7 out
of 8 in the Crystal Structure of Isocitrate Lyase-1 From Candida Albicans
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 Isocitrate Lyase-1 From Candida Albicans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg601
b:62.5
occ:1.00
|
O
|
G:HOH716
|
1.6
|
56.2
|
1.0
|
OD2
|
G:ASP172
|
2.2
|
70.4
|
1.0
|
O
|
G:HOH701
|
2.2
|
52.0
|
1.0
|
O
|
G:HOH727
|
2.4
|
54.5
|
1.0
|
OD2
|
G:ASP118
|
3.3
|
72.0
|
1.0
|
O2
|
G:FMT602
|
3.3
|
76.2
|
1.0
|
CG
|
G:ASP172
|
3.4
|
63.3
|
1.0
|
C
|
G:FMT602
|
3.6
|
80.0
|
1.0
|
N
|
G:TRP103
|
3.6
|
68.6
|
1.0
|
OD1
|
G:ASP118
|
3.9
|
75.0
|
1.0
|
N
|
G:GLY102
|
3.9
|
66.3
|
1.0
|
CG
|
G:ASP118
|
4.0
|
74.1
|
1.0
|
CA
|
G:GLY102
|
4.0
|
71.9
|
1.0
|
OD1
|
G:ASP172
|
4.1
|
62.3
|
1.0
|
NZ
|
G:LYS208
|
4.2
|
72.8
|
1.0
|
C
|
G:GLY102
|
4.2
|
70.0
|
1.0
|
OD1
|
G:ASP174
|
4.4
|
55.7
|
1.0
|
CB
|
G:TRP103
|
4.4
|
75.1
|
1.0
|
OH
|
G:TYR99
|
4.4
|
58.5
|
1.0
|
O1
|
G:FMT602
|
4.4
|
69.0
|
1.0
|
CB
|
G:ASP172
|
4.5
|
60.6
|
1.0
|
CA
|
G:TRP103
|
4.5
|
71.4
|
1.0
|
OE1
|
G:GLU201
|
4.6
|
81.5
|
1.0
|
NH1
|
G:ARG247
|
4.7
|
68.8
|
1.0
|
OG
|
G:SER101
|
4.7
|
77.0
|
1.0
|
CE1
|
G:HIS199
|
4.9
|
63.5
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 7ebe
Go back to
Magnesium Binding Sites List in 7ebe
Magnesium binding site 8 out
of 8 in the Crystal Structure of Isocitrate Lyase-1 From Candida Albicans
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 Isocitrate Lyase-1 From Candida Albicans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg601
b:70.4
occ:1.00
|
O
|
H:HOH716
|
2.1
|
63.5
|
1.0
|
OD2
|
H:ASP172
|
2.1
|
69.9
|
1.0
|
O
|
H:HOH725
|
2.7
|
42.0
|
1.0
|
O1
|
H:FMT602
|
3.1
|
68.6
|
1.0
|
OH
|
H:TYR99
|
3.2
|
65.2
|
1.0
|
O
|
H:HOH705
|
3.2
|
61.4
|
1.0
|
CG
|
H:ASP172
|
3.3
|
63.7
|
1.0
|
O2
|
H:FMT602
|
3.4
|
71.7
|
1.0
|
CE1
|
H:HIS199
|
3.6
|
62.1
|
1.0
|
C
|
H:FMT602
|
3.7
|
76.2
|
1.0
|
NH1
|
H:ARG247
|
3.8
|
70.3
|
1.0
|
NE2
|
H:HIS199
|
3.9
|
61.1
|
1.0
|
OD1
|
H:ASP172
|
3.9
|
69.3
|
1.0
|
OE2
|
H:GLU201
|
4.1
|
82.9
|
1.0
|
CB
|
H:ASP172
|
4.3
|
60.9
|
1.0
|
CH2
|
H:TRP400
|
4.5
|
63.3
|
1.0
|
N
|
H:GLY102
|
4.5
|
59.0
|
1.0
|
CZ
|
H:TYR99
|
4.5
|
68.1
|
1.0
|
OD2
|
H:ASP118
|
4.7
|
74.5
|
1.0
|
OG1
|
H:THR464
|
4.7
|
81.2
|
1.0
|
NZ
|
H:LYS208
|
4.8
|
94.1
|
1.0
|
ND1
|
H:HIS199
|
4.9
|
61.9
|
1.0
|
N
|
H:TRP103
|
4.9
|
67.8
|
1.0
|
CZ
|
H:ARG247
|
5.0
|
72.5
|
1.0
|
|
Reference:
K.Hiragi,
K.Nishio,
S.Moriyama,
T.Hamaguchi,
A.Mizoguchi,
K.Yonekura,
K.Tani,
T.Mizushima.
Structural Insights Into the Targeting Specificity of Ubiquitin Ligase For S. Cerevisiae Isocitrate Lyase But Not C. Albicans Isocitrate Lyase. J.Struct.Biol. V. 213 07748 2021.
ISSN: ESSN 1095-8657
PubMed: 34033899
DOI: 10.1016/J.JSB.2021.107748
Page generated: Wed Oct 2 20:34:17 2024
|