Sodium in PDB 3qvi: Crystal Structure of Kni-10395 Bound Histo-Aspartic Protease (Hap) From Plasmodium Falciparum

The structure of Crystal Structure of Kni-10395 Bound Histo-Aspartic Protease (Hap) From Plasmodium Falciparum, PDB code: 3qvi was solved by P.Bhaumik, A.Gustchina, A.Wlodawer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.72 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	88.430, 90.510, 192.410, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 25.2

The binding sites of Sodium atom in the Crystal Structure of Kni-10395 Bound Histo-Aspartic Protease (Hap) From Plasmodium Falciparum (pdb code 3qvi). 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 Crystal Structure of Kni-10395 Bound Histo-Aspartic Protease (Hap) From Plasmodium Falciparum, PDB code: 3qvi:

Sodium binding site 1 out of 1 in the Crystal Structure of Kni-10395 Bound Histo-Aspartic Protease (Hap) From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Kni-10395 Bound Histo-Aspartic Protease (Hap) From Plasmodium Falciparum within 5.0Å range: probe atom residue distance (Å) B Occ D:Na329 b:22.4 occ:1.00 NH2 D:ARG261 3.0 22.4 1.0 O B:HOH356 3.2 12.4 1.0 O D:HOH347 3.3 9.8 1.0 NE D:ARG261 3.4 22.9 1.0 NH2 B:ARG261 3.4 26.8 1.0 NE B:ARG261 3.6 29.5 1.0 CZ D:ARG261 3.7 25.1 1.0 C1 D:PG4334 3.8 65.2 1.0 CZ B:ARG261 4.0 28.3 1.0 O1 D:PG4334 4.2 65.2 1.0 CB B:ARG261 4.5 27.5 1.0 CB D:ARG261 4.6 22.9 1.0 CD D:ARG261 4.6 21.4 1.0 CG B:ARG261 4.7 29.5 1.0 CD B:ARG261 4.7 27.4 1.0 CG D:ARG261 4.9 23.1 1.0 C2 D:PG4334 4.9 66.6 1.0 NE2 D:HIS198 5.0 21.2 1.0 OD2 D:ASP195 5.0 33.0 1.0

P.Bhaumik, H.Xiao, K.Hidaka, A.Gustchina, Y.Kiso, R.Y.Yada, A.Wlodawer. Structural Insights Into the Activation and Inhibition of Histo-Aspartic Protease From Plasmodium Falciparum. Biochemistry V. 50 8862 2011.
ISSN: ISSN 0006-2960
PubMed: 21928835
DOI: 10.1021/BI201118Z