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Magnesium in PDB 1p9b: Structure of Fully Ligated Adenylosuccinate Synthetase From Plasmodium Falciparum

Enzymatic activity of Structure of Fully Ligated Adenylosuccinate Synthetase From Plasmodium Falciparum

All present enzymatic activity of Structure of Fully Ligated Adenylosuccinate Synthetase From Plasmodium Falciparum:
6.3.4.4;

Protein crystallography data

The structure of Structure of Fully Ligated Adenylosuccinate Synthetase From Plasmodium Falciparum, PDB code: 1p9b was solved by K.Eaazhisai, R.Jayalakshmi, P.Gayathri, R.P.Anand, K.Sumathy, H.Balaram, M.R.Murthy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.91 / 2.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 91.579, 117.117, 80.416, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 24.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Fully Ligated Adenylosuccinate Synthetase From Plasmodium Falciparum (pdb code 1p9b). 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 Structure of Fully Ligated Adenylosuccinate Synthetase From Plasmodium Falciparum, PDB code: 1p9b:

Magnesium binding site 1 out of 1 in 1p9b

Go back to Magnesium Binding Sites List in 1p9b
Magnesium binding site 1 out of 1 in the Structure of Fully Ligated Adenylosuccinate Synthetase From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Fully Ligated Adenylosuccinate Synthetase From Plasmodium Falciparum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1600

b:20.1
occ:1.00
O2A A:GDP1603 2.2 29.8 1.0
O1 A:IMO1601 2.2 18.4 1.0
OD1 A:ASP26 2.2 18.2 1.0
O2B A:GDP1603 2.3 22.0 1.0
O A:HDA1602 2.3 17.6 1.0
O A:GLY53 2.3 17.0 1.0
PB A:GDP1603 3.3 26.3 1.0
O3A A:GDP1603 3.3 30.0 1.0
PA A:GDP1603 3.3 30.9 1.0
C A:HDA1602 3.4 19.2 1.0
P A:IMO1601 3.4 19.4 1.0
CG A:ASP26 3.4 19.4 1.0
C A:GLY53 3.4 16.6 1.0
O3 A:IMO1601 3.4 17.8 1.0
CA A:ASP26 3.7 17.7 1.0
N A:GLY53 3.9 15.8 1.0
N A:ASP26 3.9 16.6 1.0
CB A:ASP26 3.9 17.6 1.0
CA A:GLY53 4.0 17.1 1.0
OG1 A:THR307 4.0 18.9 1.0
NH2 A:ARG313 4.0 14.7 1.0
OB A:HDA1602 4.0 18.8 1.0
NA A:HDA1602 4.1 20.4 1.0
CD2 A:HIS54 4.1 17.2 1.0
N1 A:IMO1601 4.1 18.6 1.0
O1B A:GDP1603 4.2 23.0 1.0
O1A A:GDP1603 4.3 29.1 1.0
OD2 A:ASP26 4.4 18.1 1.0
O2 A:IMO1601 4.4 19.0 1.0
CB A:THR307 4.4 19.7 1.0
O6 A:IMO1601 4.4 17.8 1.0
N A:HIS54 4.4 18.2 1.0
O5' A:GDP1603 4.5 32.4 1.0
O3B A:GDP1603 4.5 25.1 1.0
C6 A:IMO1601 4.6 18.8 1.0
CA A:HIS54 4.7 17.8 1.0
NE2 A:HIS54 4.8 18.7 1.0
NZ A:LYS29 5.0 19.4 1.0

Reference:

K.Eaazhisai, R.Jayalakshmi, P.Gayathri, R.P.Anand, K.Sumathy, H.Balaram, M.R.Murthy. Crystal Structure of Fully Ligated Adenylosuccinate Synthetase From Plasmodium Falciparum. J.Mol.Biol. V. 335 1251 2004.
ISSN: ISSN 0022-2836
PubMed: 14729341
DOI: 10.1016/J.JMB.2003.11.036
Page generated: Tue Aug 13 10:49:48 2024

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