Atomistry » Magnesium » PDB 3dtu-3e35 » 3e27
Atomistry »
  Magnesium »
    PDB 3dtu-3e35 »
      3e27 »

Magnesium in PDB 3e27: Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex

Enzymatic activity of Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex

All present enzymatic activity of Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex:
2.7.7.18;

Protein crystallography data

The structure of Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex, PDB code: 3e27 was solved by D.Martynowski, Y.Eyobo, H.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.856, 137.413, 143.972, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 27.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex (pdb code 3e27). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex, PDB code: 3e27:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 3e27

Go back to Magnesium Binding Sites List in 3e27
Magnesium binding site 1 out of 4 in the Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg190

b:40.3
occ:1.00
 OD1 A:ASP108 2.6 23.1 1.0
O14 A:DND191 3.0 25.3 1.0
NH2 A:ARG133 3.1 32.2 1.0
O12 A:DND191 3.1 31.1 1.0
C2B A:DND191 3.3 24.0 1.0
CG A:ASP108 3.5 26.2 1.0
O2B A:DND191 3.6 23.5 1.0
OD2 A:ASP108 3.6 26.4 1.0
PA A:DND191 3.8 24.9 1.0
O5B A:DND191 3.9 25.2 1.0
C3B A:DND191 4.0 24.5 1.0
O A:HOH230 4.1 35.8 1.0
PN A:DND191 4.2 26.4 1.0
O3P A:DND191 4.2 26.7 1.0
O A:HOH227 4.4 33.0 1.0
CZ A:ARG133 4.4 33.6 1.0
C8A A:DND191 4.4 23.2 1.0
CG A:MET109 4.5 27.3 1.0
C1B A:DND191 4.6 23.2 1.0
N9A A:DND191 4.7 24.6 1.0
O A:HOH226 4.9 27.4 1.0
CB A:ASP108 4.9 26.0 1.0
C5B A:DND191 4.9 23.8 1.0
C4B A:DND191 5.0 24.0 1.0

Magnesium binding site 2 out of 4 in 3e27

Go back to Magnesium Binding Sites List in 3e27
Magnesium binding site 2 out of 4 in the Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg190

b:36.8
occ:1.00
 O12 B:DND191 2.6 30.2 1.0
OD1 B:ASP108 2.7 27.9 1.0
O B:HOH294 3.1 32.5 1.0
O14 B:DND191 3.3 29.4 1.0
NH2 B:ARG133 3.3 42.5 1.0
O B:HOH297 3.4 39.9 1.0
C2B B:DND191 3.4 25.2 1.0
CG B:ASP108 3.6 27.3 1.0
O2B B:DND191 3.6 26.7 1.0
O5B B:DND191 3.8 27.1 1.0
OD2 B:ASP108 3.8 26.9 1.0
PN B:DND191 3.8 28.3 1.0
PA B:DND191 3.9 27.6 1.0
C3B B:DND191 4.0 23.7 1.0
O3P B:DND191 4.0 28.9 1.0
O B:HOH295 4.1 28.2 1.0
CG B:MET109 4.2 24.1 1.0
CE B:MET109 4.4 18.4 1.0
CZ B:ARG133 4.6 39.6 1.0
C8A B:DND191 4.6 26.0 1.0
O11 B:DND191 4.7 29.3 1.0
C1B B:DND191 4.7 25.5 1.0
C5B B:DND191 4.8 23.9 1.0
O B:HOH270 4.9 29.5 1.0
N9A B:DND191 4.9 26.8 1.0
C4B B:DND191 4.9 25.0 1.0
O5D B:DND191 4.9 27.4 1.0
CB B:ASP108 5.0 25.8 1.0

Magnesium binding site 3 out of 4 in 3e27

Go back to Magnesium Binding Sites List in 3e27
Magnesium binding site 3 out of 4 in the Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg190

b:40.9
occ:1.00
 OD1 C:ASP108 2.6 20.4 1.0
O12 C:DND191 2.9 25.3 1.0
O C:HOH256 2.9 38.7 1.0
O14 C:DND191 3.2 21.7 1.0
C2B C:DND191 3.4 19.3 1.0
CG C:ASP108 3.4 22.1 1.0
NH2 C:ARG133 3.4 32.4 1.0
OD2 C:ASP108 3.5 22.7 1.0
O C:HOH287 3.6 34.6 1.0
O2B C:DND191 3.6 17.5 1.0
C3B C:DND191 3.9 18.6 1.0
O5B C:DND191 3.9 21.2 1.0
O C:HOH226 4.0 26.9 1.0
PA C:DND191 4.0 22.2 1.0
PN C:DND191 4.1 24.1 1.0
CE C:MET109 4.3 20.3 1.0
O3P C:DND191 4.3 22.6 1.0
C8A C:DND191 4.5 23.0 1.0
CG C:MET109 4.6 19.9 1.0
C1B C:DND191 4.6 20.9 1.0
CZ C:ARG133 4.7 31.7 1.0
CB C:ASP108 4.8 22.0 1.0
O C:HOH291 4.8 29.5 1.0
N9A C:DND191 4.8 22.2 1.0
C4B C:DND191 4.9 19.5 1.0
C5B C:DND191 4.9 20.1 1.0
O3B C:DND191 4.9 17.4 1.0
O11 C:DND191 4.9 25.3 1.0

Magnesium binding site 4 out of 4 in 3e27

Go back to Magnesium Binding Sites List in 3e27
Magnesium binding site 4 out of 4 in the Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Nicotinic Acid Mononucleotide (Namn) Adenylyltransferase From Bacillus Anthracis: Product Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg190

b:39.6
occ:1.00
 O D:HOH297 2.4 30.1 1.0
OD1 D:ASP108 2.5 25.5 1.0
O12 D:DND191 3.0 32.0 1.0
C2B D:DND191 3.3 20.6 1.0
CG D:ASP108 3.4 26.8 1.0
NH2 D:ARG133 3.5 37.2 1.0
O14 D:DND191 3.5 26.4 1.0
O2B D:DND191 3.5 22.2 1.0
OD2 D:ASP108 3.6 27.9 1.0
O5B D:DND191 3.8 22.1 1.0
C3B D:DND191 3.9 20.7 1.0
PA D:DND191 4.0 26.0 1.0
PN D:DND191 4.1 28.8 1.0
O3P D:DND191 4.1 29.1 1.0
O D:HOH295 4.3 32.1 1.0
CG D:MET109 4.4 24.4 1.0
C8A D:DND191 4.5 22.4 1.0
C1B D:DND191 4.6 21.3 1.0
CE D:MET109 4.6 22.4 1.0
N9A D:DND191 4.7 23.0 1.0
CZ D:ARG133 4.8 38.2 1.0
CB D:ASP108 4.9 26.1 1.0
O3B D:DND191 4.9 20.1 1.0
C5B D:DND191 4.9 20.2 1.0
C4B D:DND191 4.9 18.1 1.0

Reference:

L.Sorci, Y.Pan, Y.Eyobo, I.Rodionova, N.Huang, O.Kurnasov, S.Zhong, A.D.Mackerell, H.Zhang, A.L.Osterman. Targeting Nad Biosynthesis in Bacterial Pathogens: Structure-Based Development of Inhibitors of Nicotinate Mononucleotide Adenylyltransferase Nadd. Chem.Biol. V. 16 849 2009.
ISSN: ISSN 1074-5521
PubMed: 19716475
DOI: 10.1016/J.CHEMBIOL.2009.07.006
Page generated: Wed Aug 14 12:50:22 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy