Sodium in PDB 4hqo: Crystal Structure of Plasmodium Vivax Trap Protein

The structure of Crystal Structure of Plasmodium Vivax Trap Protein, PDB code: 4hqo was solved by G.Song, A.C.Koksal, C.Lu, T.A.Springer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.43 / 2.19
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.294, 100.474, 158.547, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 20

The structure of Crystal Structure of Plasmodium Vivax Trap Protein also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Chlorine	(Cl)	2 atoms

The binding sites of Sodium atom in the Crystal Structure of Plasmodium Vivax Trap Protein (pdb code 4hqo). 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 Plasmodium Vivax Trap Protein, PDB code: 4hqo:

Sodium binding site 1 out of 1 in the Crystal Structure of Plasmodium Vivax Trap Protein


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 Plasmodium Vivax Trap Protein within 5.0Å range: probe atom residue distance (Å) B Occ A:Na305 b:53.7 occ:1.00 OE1 A:GLU95 2.2 64.2 1.0 OH A:TYR85 2.3 30.1 1.0 CZ A:TYR85 3.1 30.8 1.0 O A:HOH551 3.1 76.2 1.0 CE2 A:TYR85 3.1 22.9 1.0 CD A:GLU95 3.1 56.0 1.0 OE2 A:GLU135 3.4 54.4 1.0 CG A:GLU95 3.5 35.5 1.0 CD A:GLU135 3.5 51.9 1.0 CB A:GLU95 3.6 32.7 1.0 CB A:GLU135 3.7 29.4 1.0 CG A:GLU135 3.7 44.8 1.0 ND2 A:ASN87 3.9 47.2 1.0 OE1 A:GLU135 4.0 70.5 1.0 CE1 A:HIS139 4.1 37.5 1.0 O A:HOH665 4.1 81.1 1.0 OE2 A:GLU95 4.3 57.6 1.0 CE1 A:TYR85 4.4 29.4 1.0 O A:HOH426 4.4 41.4 1.0 CD2 A:TYR85 4.5 23.7 1.0 CA A:GLU95 4.6 23.1 1.0 O A:HOH631 4.7 74.9 1.0 CA A:GLU135 4.8 37.1 1.0 ND1 A:HIS139 4.9 37.2 1.0 NH2 A:ARG98 4.9 62.4 1.0

G.Song, A.C.Koksal, C.Lu, T.A.Springer. Shape Change in the Receptor For Gliding Motility in Plasmodium Sporozoites. Proc.Natl.Acad.Sci.Usa V. 109 21420 2012.
ISSN: ISSN 0027-8424
PubMed: 23236185
DOI: 10.1073/PNAS.1218581109