Magnesium in PDB 7mgq: Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans
Enzymatic activity of Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans
All present enzymatic activity of Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans:
2.1.2.3;
3.5.4.10;
Protein crystallography data
The structure of Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans, PDB code: 7mgq
was solved by
M.S.Wizrah,
S.M.H.Chua,
Z.Luo,
M.K.Manik,
M.Pan,
J.M.Whyte,
A.B.Robertson,
U.Kappler,
B.Kobe,
J.A.Fraser,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.92 /
2.67
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
91.841,
115.867,
111.823,
90,
96.18,
90
|
R / Rfree (%)
|
19.9 /
23.5
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans
(pdb code 7mgq). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the
Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans, PDB code: 7mgq:
Jump to Magnesium binding site number:
1;
2;
3;
4;
Magnesium binding site 1 out
of 4 in 7mgq
Go back to
Magnesium Binding Sites List in 7mgq
Magnesium binding site 1 out
of 4 in the Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg701
b:42.8
occ:1.00
|
O
|
A:LEU436
|
2.4
|
56.3
|
1.0
|
O
|
A:LEU602
|
2.6
|
62.7
|
1.0
|
O
|
A:THR439
|
2.6
|
50.0
|
1.0
|
OG
|
A:SER441
|
2.9
|
61.9
|
1.0
|
OG
|
A:SER443
|
3.1
|
52.0
|
1.0
|
OD2
|
A:ASP552
|
3.3
|
63.0
|
1.0
|
C
|
A:LEU436
|
3.5
|
53.6
|
1.0
|
C
|
A:THR439
|
3.7
|
51.0
|
1.0
|
N
|
A:HIS604
|
3.7
|
57.6
|
1.0
|
C
|
A:LEU602
|
3.8
|
62.2
|
1.0
|
CB
|
A:HIS604
|
3.8
|
54.0
|
1.0
|
CB
|
A:ASP552
|
4.0
|
61.1
|
1.0
|
CB
|
A:SER441
|
4.1
|
59.9
|
1.0
|
CG
|
A:ASP552
|
4.1
|
62.7
|
1.0
|
CA
|
A:SER441
|
4.2
|
57.5
|
1.0
|
CA
|
A:LEU436
|
4.2
|
52.3
|
1.0
|
N
|
A:SER441
|
4.2
|
53.7
|
1.0
|
C
|
A:PHE603
|
4.3
|
60.9
|
1.0
|
CB
|
A:SER443
|
4.3
|
52.9
|
1.0
|
CA
|
A:PHE603
|
4.3
|
59.2
|
1.0
|
N
|
A:THR439
|
4.3
|
51.3
|
1.0
|
C
|
A:GLN440
|
4.4
|
54.6
|
1.0
|
CA
|
A:THR439
|
4.4
|
50.5
|
1.0
|
CA
|
A:HIS604
|
4.4
|
56.3
|
1.0
|
CB
|
A:THR439
|
4.4
|
52.2
|
1.0
|
CB
|
A:LEU436
|
4.5
|
53.6
|
1.0
|
N
|
A:PHE603
|
4.5
|
60.0
|
1.0
|
N
|
A:LYS437
|
4.6
|
53.7
|
1.0
|
O
|
A:GLN440
|
4.6
|
55.2
|
1.0
|
CB
|
A:LEU602
|
4.7
|
59.1
|
1.0
|
C
|
A:LYS437
|
4.7
|
48.8
|
1.0
|
CA
|
A:LYS437
|
4.8
|
51.2
|
1.0
|
N
|
A:GLN440
|
4.8
|
50.7
|
1.0
|
O
|
A:LYS437
|
4.8
|
50.5
|
1.0
|
O
|
A:HIS604
|
4.8
|
53.3
|
1.0
|
CA
|
A:LEU602
|
4.9
|
61.2
|
1.0
|
CA
|
A:GLN440
|
5.0
|
53.5
|
1.0
|
N
|
A:SER443
|
5.0
|
57.4
|
1.0
|
|
Magnesium binding site 2 out
of 4 in 7mgq
Go back to
Magnesium Binding Sites List in 7mgq
Magnesium binding site 2 out
of 4 in the Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg701
b:50.5
occ:1.00
|
O
|
B:LEU436
|
2.4
|
56.1
|
1.0
|
O
|
B:THR439
|
2.5
|
55.7
|
1.0
|
O
|
B:LEU602
|
2.6
|
66.1
|
1.0
|
OG
|
B:SER443
|
3.0
|
63.9
|
1.0
|
OG
|
B:SER441
|
3.0
|
65.0
|
1.0
|
OD2
|
B:ASP552
|
3.2
|
61.6
|
1.0
|
C
|
B:LEU436
|
3.5
|
56.2
|
1.0
|
C
|
B:THR439
|
3.6
|
56.5
|
1.0
|
N
|
B:HIS604
|
3.8
|
59.4
|
1.0
|
C
|
B:LEU602
|
3.8
|
65.5
|
1.0
|
CB
|
B:HIS604
|
3.8
|
60.1
|
1.0
|
CB
|
B:ASP552
|
4.0
|
62.9
|
1.0
|
CG
|
B:ASP552
|
4.1
|
62.5
|
1.0
|
CB
|
B:SER441
|
4.2
|
62.9
|
1.0
|
CA
|
B:LEU436
|
4.2
|
57.6
|
1.0
|
N
|
B:THR439
|
4.2
|
56.8
|
1.0
|
CB
|
B:SER443
|
4.2
|
62.6
|
1.0
|
C
|
B:PHE603
|
4.2
|
60.2
|
1.0
|
CA
|
B:THR439
|
4.2
|
55.7
|
1.0
|
N
|
B:SER441
|
4.3
|
58.2
|
1.0
|
CA
|
B:PHE603
|
4.3
|
63.0
|
1.0
|
CA
|
B:SER441
|
4.3
|
59.7
|
1.0
|
CB
|
B:THR439
|
4.3
|
56.2
|
1.0
|
C
|
B:GLN440
|
4.3
|
60.5
|
1.0
|
CA
|
B:HIS604
|
4.4
|
60.0
|
1.0
|
CB
|
B:LEU436
|
4.5
|
57.1
|
1.0
|
N
|
B:PHE603
|
4.5
|
66.3
|
1.0
|
O
|
B:GLN440
|
4.5
|
64.7
|
1.0
|
N
|
B:LYS437
|
4.5
|
56.6
|
1.0
|
N
|
B:GLN440
|
4.7
|
57.6
|
1.0
|
C
|
B:LYS437
|
4.7
|
56.9
|
1.0
|
O
|
B:LYS437
|
4.7
|
57.3
|
1.0
|
CB
|
B:LEU602
|
4.7
|
63.1
|
1.0
|
CA
|
B:LYS437
|
4.7
|
57.1
|
1.0
|
O
|
B:HIS604
|
4.9
|
60.8
|
1.0
|
CA
|
B:LEU602
|
4.9
|
64.8
|
1.0
|
CA
|
B:GLN440
|
4.9
|
58.8
|
1.0
|
N
|
B:SER443
|
5.0
|
63.8
|
1.0
|
CG
|
B:HIS604
|
5.0
|
60.4
|
1.0
|
|
Magnesium binding site 3 out
of 4 in 7mgq
Go back to
Magnesium Binding Sites List in 7mgq
Magnesium binding site 3 out
of 4 in the Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg701
b:54.0
occ:1.00
|
O
|
C:LEU436
|
2.5
|
52.0
|
1.0
|
O
|
C:THR439
|
2.5
|
55.3
|
1.0
|
O
|
C:LEU602
|
2.5
|
59.6
|
1.0
|
OG
|
C:SER441
|
2.9
|
56.5
|
1.0
|
OG
|
C:SER443
|
3.2
|
64.6
|
1.0
|
OD2
|
C:ASP552
|
3.3
|
59.5
|
1.0
|
CB
|
C:HIS604
|
3.5
|
59.9
|
1.0
|
N
|
C:HIS604
|
3.5
|
63.4
|
1.0
|
C
|
C:LEU436
|
3.6
|
51.7
|
1.0
|
C
|
C:THR439
|
3.6
|
57.5
|
1.0
|
C
|
C:LEU602
|
3.7
|
60.9
|
1.0
|
CB
|
C:ASP552
|
4.0
|
55.7
|
1.0
|
C
|
C:PHE603
|
4.0
|
63.4
|
1.0
|
CA
|
C:HIS604
|
4.1
|
61.6
|
1.0
|
N
|
C:SER441
|
4.1
|
61.2
|
1.0
|
CB
|
C:SER441
|
4.1
|
58.3
|
1.0
|
CG
|
C:ASP552
|
4.1
|
58.4
|
1.0
|
CA
|
C:PHE603
|
4.2
|
61.0
|
1.0
|
CA
|
C:SER441
|
4.2
|
61.3
|
1.0
|
N
|
C:THR439
|
4.3
|
57.0
|
1.0
|
C
|
C:GLN440
|
4.3
|
61.0
|
1.0
|
CB
|
C:SER443
|
4.3
|
60.5
|
1.0
|
CA
|
C:LEU436
|
4.4
|
51.7
|
1.0
|
CA
|
C:THR439
|
4.4
|
56.8
|
1.0
|
N
|
C:PHE603
|
4.4
|
57.9
|
1.0
|
CB
|
C:THR439
|
4.5
|
57.4
|
1.0
|
O
|
C:GLN440
|
4.6
|
63.3
|
1.0
|
N
|
C:LYS437
|
4.6
|
53.8
|
1.0
|
O
|
C:HIS604
|
4.6
|
60.9
|
1.0
|
O
|
C:LYS437
|
4.6
|
54.0
|
1.0
|
N
|
C:GLN440
|
4.6
|
57.7
|
1.0
|
C
|
C:LYS437
|
4.7
|
53.7
|
1.0
|
CB
|
C:LEU436
|
4.7
|
51.5
|
1.0
|
CB
|
C:LEU602
|
4.7
|
57.3
|
1.0
|
CG
|
C:HIS604
|
4.7
|
62.4
|
1.0
|
CA
|
C:LYS437
|
4.7
|
51.7
|
1.0
|
CA
|
C:GLN440
|
4.8
|
61.4
|
1.0
|
CA
|
C:LEU602
|
4.9
|
60.4
|
1.0
|
C
|
C:HIS604
|
4.9
|
63.4
|
1.0
|
O
|
C:PHE603
|
4.9
|
68.8
|
1.0
|
|
Magnesium binding site 4 out
of 4 in 7mgq
Go back to
Magnesium Binding Sites List in 7mgq
Magnesium binding site 4 out
of 4 in the Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg701
b:62.9
occ:1.00
|
O
|
D:THR439
|
2.5
|
60.1
|
1.0
|
O
|
D:LEU436
|
2.6
|
64.9
|
1.0
|
O
|
D:LEU602
|
2.7
|
71.0
|
1.0
|
OG
|
D:SER443
|
3.0
|
71.3
|
1.0
|
OD2
|
D:ASP552
|
3.0
|
69.0
|
1.0
|
O
|
D:SER441
|
3.1
|
72.0
|
1.0
|
N
|
D:HIS604
|
3.6
|
70.5
|
1.0
|
C
|
D:THR439
|
3.6
|
61.1
|
1.0
|
C
|
D:LEU436
|
3.7
|
64.6
|
1.0
|
CB
|
D:HIS604
|
3.8
|
68.7
|
1.0
|
C
|
D:LEU602
|
3.9
|
72.8
|
1.0
|
CG
|
D:ASP552
|
3.9
|
70.2
|
1.0
|
CB
|
D:ASP552
|
4.0
|
70.9
|
1.0
|
CB
|
D:SER443
|
4.1
|
68.9
|
1.0
|
C
|
D:PHE603
|
4.1
|
74.3
|
1.0
|
CA
|
D:PHE603
|
4.2
|
72.7
|
1.0
|
N
|
D:THR439
|
4.2
|
59.9
|
1.0
|
CB
|
D:THR439
|
4.2
|
63.7
|
1.0
|
CA
|
D:THR439
|
4.2
|
60.8
|
1.0
|
CA
|
D:HIS604
|
4.3
|
69.8
|
1.0
|
C
|
D:SER441
|
4.3
|
72.3
|
1.0
|
CA
|
D:LEU436
|
4.3
|
61.6
|
1.0
|
N
|
D:PHE603
|
4.5
|
73.3
|
1.0
|
CB
|
D:LEU436
|
4.6
|
62.4
|
1.0
|
C
|
D:GLN440
|
4.6
|
68.6
|
1.0
|
N
|
D:SER443
|
4.7
|
69.0
|
1.0
|
O
|
D:GLN440
|
4.7
|
69.2
|
1.0
|
N
|
D:GLN440
|
4.7
|
62.5
|
1.0
|
N
|
D:LYS437
|
4.7
|
64.9
|
1.0
|
O
|
D:HIS604
|
4.8
|
70.0
|
1.0
|
C
|
D:LYS437
|
4.8
|
66.4
|
1.0
|
N
|
D:SER441
|
4.8
|
70.0
|
1.0
|
O
|
D:LYS437
|
4.9
|
70.2
|
1.0
|
CA
|
D:LYS437
|
4.9
|
66.6
|
1.0
|
C
|
D:ASN442
|
4.9
|
69.2
|
1.0
|
CB
|
D:LEU602
|
4.9
|
74.8
|
1.0
|
CG2
|
D:THR439
|
4.9
|
62.6
|
1.0
|
CA
|
D:ASN442
|
5.0
|
73.0
|
1.0
|
|
Reference:
M.S.I.Wizrah,
S.M.H.Chua,
Z.Luo,
M.K.Manik,
M.Pan,
J.M.L.Whyte,
A.A.B.Robertson,
U.Kappler,
B.Kobe,
J.A.Fraser.
Aicar Transformylase/Imp Cyclohydrolase (Atic) Is Essential For De Novo Purine Biosynthesis and Infection By Cryptococcus Neoformans. J.Biol.Chem. V. 298 02453 2022.
ISSN: ESSN 1083-351X
PubMed: 36063996
DOI: 10.1016/J.JBC.2022.102453
Page generated: Thu Oct 3 00:51:55 2024
|