Potassium in PDB 5l88: Afamin Antibody Fragment, N14 Fab, L1- Glycosilated, Crystal Form I, Non-Parsimonious Model

The structure of Afamin Antibody Fragment, N14 Fab, L1- Glycosilated, Crystal Form I, Non-Parsimonious Model, PDB code: 5l88 was solved by B.Rupp, A.Naschberger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.38 / 1.88
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	67.782, 69.249, 87.803, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 21.1

The binding sites of Potassium atom in the Afamin Antibody Fragment, N14 Fab, L1- Glycosilated, Crystal Form I, Non-Parsimonious Model (pdb code 5l88). 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 Afamin Antibody Fragment, N14 Fab, L1- Glycosilated, Crystal Form I, Non-Parsimonious Model, PDB code: 5l88:

Potassium binding site 1 out of 1 in the Afamin Antibody Fragment, N14 Fab, L1- Glycosilated, Crystal Form I, Non-Parsimonious Model


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Afamin Antibody Fragment, N14 Fab, L1- Glycosilated, Crystal Form I, Non-Parsimonious Model within 5.0Å range: probe atom residue distance (Å) B Occ H:K310 b:33.3 occ:1.00 O H:ASP207 2.9 28.0 1.0 OD2 H:ASP207 2.9 29.6 1.0 O H:HOH466 2.9 35.9 1.0 O H:HOH505 3.0 46.1 1.0 CG H:ASP207 3.7 31.3 1.0 O H:HOH481 3.9 31.4 1.0 C H:ASP207 4.0 30.9 1.0 OD1 H:ASP207 4.2 30.0 1.0 CB H:ASP207 4.4 32.9 1.0 N H:LYS209 4.5 33.1 1.0 CB H:LYS209 4.7 40.9 1.0 CA H:ASP207 4.8 31.4 1.0 N H:LYS208 4.9 30.2 1.0 CA H:LYS208 4.9 29.9 1.0

A.Naschberger, B.G.Furnrohr, T.Lenac Rovis, S.Malic, K.Scheffzek, H.Dieplinger, B.Rupp. The N14 Anti-Afamin Antibody Fab: A Rare VL1 Cdr Glycosylation, Crystallographic Re-Sequencing, Molecular Plasticity and Conservative Versus Enthusiastic Modelling. Acta Crystallogr D Struct V. 72 1267 2016BIOL.
ISSN: ISSN 2059-7983
PubMed: 27917827
DOI: 10.1107/S205979831601723X