Potassium in PDB 4kmy: Human Folate Receptor Beta (FOLR2) at Neutral pH

The structure of Human Folate Receptor Beta (FOLR2) at Neutral pH, PDB code: 4kmy was solved by A.S.Wibowo, C.E.Dann Iii, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.51 / 1.80
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	75.026, 75.026, 97.188, 90.00, 90.00, 120.00
R / Rfree (%)	16.4 / 19.3

The binding sites of Potassium atom in the Human Folate Receptor Beta (FOLR2) at Neutral pH (pdb code 4kmy). 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 Human Folate Receptor Beta (FOLR2) at Neutral pH, PDB code: 4kmy:

Potassium binding site 1 out of 1 in the Human Folate Receptor Beta (FOLR2) at Neutral pH


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Human Folate Receptor Beta (FOLR2) at Neutral pH within 5.0Å range: probe atom residue distance (Å) B Occ A:K301 b:26.7 occ:1.00 OG A:SER104 3.1 22.6 1.0 NE1 A:TRP54 3.2 22.2 1.0 ND2 A:ASN216 3.3 21.6 1.0 ND2 A:ASN214 3.3 28.9 1.0 OD1 A:ASN106 3.4 30.6 1.0 CB A:ASN216 3.7 25.0 1.0 OD1 A:ASN214 3.7 31.6 1.0 CB A:SER104 3.7 19.7 1.0 CD1 A:TRP54 3.9 25.1 1.0 CG A:ASN214 3.9 31.3 1.0 CG A:ASN216 4.0 24.2 1.0 CD1 A:LEU100 4.1 21.2 1.0 CA A:SER104 4.1 19.6 1.0 CB A:ASN106 4.1 22.8 1.0 CG A:ASN106 4.1 27.8 1.0 CZ A:PHE208 4.2 25.8 1.0 CE1 A:PHE208 4.2 27.7 1.0 CD A:PRO105 4.3 28.1 1.0 CE2 A:TRP54 4.3 22.8 1.0 N A:ASN106 4.7 24.5 1.0 N A:PRO105 4.7 24.7 1.0 CZ2 A:TRP54 4.8 22.6 1.0 C A:SER104 4.9 23.5 1.0 CA A:ASN216 5.0 24.8 1.0 CA A:ASN106 5.0 25.1 1.0

A.S.Wibowo, M.Singh, K.M.Reeder, J.J.Carter, A.R.Kovach, W.Meng, M.Ratnam, F.Zhang, C.E.Dann. Structures of Human Folate Receptors Reveal Biological Trafficking States and Diversity in Folate and Antifolate Recognition. Proc.Natl.Acad.Sci.Usa V. 110 15180 2013.
ISSN: ISSN 0027-8424
PubMed: 23934049
DOI: 10.1073/PNAS.1308827110