Potassium in PDB 3kas: Machupo Virus GP1 Bound to Human Transferrin Receptor 1

The structure of Machupo Virus GP1 Bound to Human Transferrin Receptor 1, PDB code: 3kas was solved by J.Abraham, K.D.Corbett, S.C.Harrison, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.13 / 2.40
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	143.951, 170.228, 98.471, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 23.8

The binding sites of Potassium atom in the Machupo Virus GP1 Bound to Human Transferrin Receptor 1 (pdb code 3kas). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Machupo Virus GP1 Bound to Human Transferrin Receptor 1, PDB code: 3kas:

Potassium binding site 1 out of 1 in the Machupo Virus GP1 Bound to Human Transferrin Receptor 1


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Machupo Virus GP1 Bound to Human Transferrin Receptor 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:K1 b:54.8 occ:1.00 N A:GLN443 3.3 42.7 1.0 N A:LEU122 3.4 40.5 1.0 O A:HOH773 3.5 64.0 1.0 ND1 A:HIS603 3.7 39.2 1.0 CD1 A:PHE442 3.8 38.6 1.0 O A:GLN443 3.9 44.9 1.0 CE1 A:HIS603 3.9 42.2 1.0 CA A:GLN443 4.0 38.1 1.0 CA A:ARG121 4.0 52.2 1.0 CB A:LEU122 4.1 39.2 1.0 CB A:GLN443 4.1 41.8 1.0 CD1 A:LEU127 4.1 44.3 1.0 C A:GLN443 4.1 35.9 1.0 CA A:PHE442 4.1 42.4 1.0 C A:PHE442 4.2 45.7 1.0 C A:ARG121 4.2 46.6 1.0 CA A:LEU122 4.2 42.4 1.0 O A:LEU122 4.3 44.4 1.0 CG A:LEU122 4.3 42.6 1.0 CG A:ARG121 4.4 60.9 1.0 O A:GLY441 4.4 45.8 1.0 CE1 A:PHE442 4.4 34.0 1.0 C A:LEU122 4.6 43.6 1.0 CB A:ARG121 4.7 56.8 1.0 CG A:GLN443 4.7 48.9 1.0 NH1 A:ARG121 4.7 64.7 1.0 CD1 A:LEU122 4.8 40.6 1.0 CD2 A:LEU127 4.8 43.7 1.0 CG A:LEU127 4.9 44.7 1.0 CG A:PHE442 4.9 34.8 1.0

J.Abraham, K.D.Corbett, M.Farzan, H.Choe, S.C.Harrison. Structural Basis For Receptor Recognition By New World Hemorrhagic Fever Arenaviruses. Nat.Struct.Mol.Biol. V. 17 438 2010.
ISSN: ISSN 1545-9993
PubMed: 20208545
DOI: 10.1038/NSMB.1772