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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

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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

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