Sodium in PDB 2ok7: Ferredoxin-Nadp+ Reductase From Plasmodium Falciparum with 2'P-Amp

All present enzymatic activity of Ferredoxin-Nadp+ Reductase From Plasmodium Falciparum with 2'P-Amp:
1.18.1.2;

The structure of Ferredoxin-Nadp+ Reductase From Plasmodium Falciparum with 2'P-Amp, PDB code: 2ok7 was solved by M.Milani, E.Mastrangelo, M.Bolognesi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.70
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	123.129, 123.129, 133.807, 90.00, 90.00, 120.00
R / Rfree (%)	26 / 32.1

The binding sites of Sodium atom in the Ferredoxin-Nadp+ Reductase From Plasmodium Falciparum with 2'P-Amp (pdb code 2ok7). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Ferredoxin-Nadp+ Reductase From Plasmodium Falciparum with 2'P-Amp, PDB code: 2ok7:

Sodium binding site 1 out of 1 in the Ferredoxin-Nadp+ Reductase From Plasmodium Falciparum with 2'P-Amp


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Ferredoxin-Nadp+ Reductase From Plasmodium Falciparum with 2'P-Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Na9001 b:2.0 occ:1.00 O4P A:A2P416 2.7 7.5 1.0 O A:HOH9028 3.0 2.0 1.0 O A:HOH9046 3.3 2.0 1.0 OG1 A:THR178 3.3 3.6 1.0 O A:THR178 3.4 2.0 1.0 CD2 A:HIS286 3.4 14.0 1.0 NE2 A:HIS286 3.5 2.0 1.0 O5' A:A2P416 3.7 2.0 1.0 P2 A:A2P416 3.7 2.0 1.0 C A:THR178 3.7 2.0 1.0 CB A:THR178 4.0 2.0 1.0 O5P A:A2P416 4.1 34.5 1.0 N A:GLY179 4.1 2.0 1.0 CA A:GLY179 4.1 2.0 1.0 C5' A:A2P416 4.2 2.0 1.0 CG A:HIS286 4.3 10.9 1.0 N A:HIS286 4.3 3.8 1.0 CA A:GLY285 4.4 2.0 1.0 CE1 A:HIS286 4.4 14.7 1.0 CA A:THR178 4.5 2.0 1.0 C A:GLY285 4.6 3.2 1.0 N A:THR180 4.6 2.0 1.0 ND1 A:HIS286 4.8 2.0 1.0 C A:GLY179 4.9 2.0 1.0 O4' A:A2P416 4.9 2.0 1.0

M.Milani, E.Balconi, A.Aliverti, E.Mastrangelo, F.Seeber, M.Bolognesi, G.Zanetti. Ferredoxin-Nadp(+) Reductase From Plasmodium Falciparum Undergoes Nadp(+)-Dependent Dimerization and Inactivation: Functional and Crystallographic Analysis. J.Mol.Biol. V. 367 501 2007.
ISSN: ISSN 0022-2836
PubMed: 17258767
DOI: 10.1016/J.JMB.2007.01.005