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Magnesium in PDB 1nht: Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K

Enzymatic activity of Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K

All present enzymatic activity of Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K:
6.3.4.4;

Protein crystallography data

The structure of Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K, PDB code: 1nht was solved by B.W.Poland, C.A.Bruns, H.J.Fromm, R.B.Honzatko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 2.50
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 80.540, 80.540, 158.150, 90.00, 90.00, 120.00
R / Rfree (%) 20.6 / 25.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K (pdb code 1nht). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K, PDB code: 1nht:

Magnesium binding site 1 out of 1 in 1nht

Go back to Magnesium Binding Sites List in 1nht
Magnesium binding site 1 out of 1 in the Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli Data Collected at 100K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg435

b:12.5
occ:1.00
 O2A A:GDP432 1.8 8.0 1.0
O1B A:GDP432 1.8 8.9 1.0
O A:HDA437 2.0 9.1 1.0
O A:GLY40 2.1 14.5 1.0
O3P A:PGS440 2.2 13.2 1.0
OD1 A:ASP13 2.8 13.0 1.0
PA A:GDP432 2.8 8.1 1.0
PB A:GDP432 3.0 9.9 1.0
C A:HDA437 3.1 9.6 1.0
O3A A:GDP432 3.2 8.4 1.0
C A:GLY40 3.3 13.9 1.0
H A:GLY40 3.4 0.0 1.0
O1A A:GDP432 3.4 9.6 1.0
CG A:ASP13 3.4 12.0 1.0
P A:PGS440 3.5 13.0 1.0
O2P A:PGS440 3.7 12.9 1.0
HH22 A:ARG305 3.7 0.0 1.0
H A:ASP13 3.8 0.0 1.0
CA A:ASP13 3.8 11.2 1.0
O3B A:GDP432 3.8 10.1 1.0
HH21 A:ARG305 3.9 0.0 1.0
CB A:ASP13 4.0 11.1 1.0
NH2 A:ARG305 4.1 17.1 1.0
HZ3 A:LYS16 4.1 0.0 1.0
NA A:HDA437 4.1 9.6 1.0
N A:GLY40 4.1 11.9 1.0
O2B A:GDP432 4.1 10.2 1.0
OD2 A:ASP13 4.1 12.2 1.0
HN1 A:PGS440 4.1 0.0 1.0
CA A:GLY40 4.2 13.0 1.0
O5' A:GDP432 4.2 7.0 1.0
N A:HIS41 4.2 14.2 1.0
HOB A:HDA437 4.2 0.0 1.0
N A:ASP13 4.2 11.6 1.0
CA A:HIS41 4.2 14.5 1.0
O1P A:PGS440 4.3 12.2 1.0
H A:ALA299 4.3 0.0 1.0
OB A:HDA437 4.4 9.9 1.0
CB A:ALA299 4.5 19.4 1.0
CD2 A:HIS41 4.7 14.0 1.0
HZ1 A:LYS16 4.7 0.0 1.0
S6 A:PGS440 4.8 12.6 1.0
NZ A:LYS16 4.8 7.0 1.0
N1 A:PGS440 5.0 10.9 1.0
C A:ASP13 5.0 11.4 1.0

Reference:

B.W.Poland, C.Bruns, H.J.Fromm, R.B.Honzatko. Entrapment of 6-Thiophosphoryl-Imp in the Active Site of Crystalline Adenylosuccinate Synthetase From Escherichia Coli. J.Biol.Chem. V. 272 15200 1997.
ISSN: ISSN 0021-9258
PubMed: 9182542
DOI: 10.1074/JBC.272.24.15200
Page generated: Tue Aug 13 10:04:14 2024

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