Potassium in PDB 2o84: Crystal Structure of K206E Mutant of N-Lobe Human Transferrin

The structure of Crystal Structure of K206E Mutant of N-Lobe Human Transferrin, PDB code: 2o84 was solved by H.M.Baker, D.Nurizzo, A.B.Mason, E.N.Baker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.02 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.173, 57.317, 135.583, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 26.9

The structure of Crystal Structure of K206E Mutant of N-Lobe Human Transferrin also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Potassium atom in the Crystal Structure of K206E Mutant of N-Lobe Human Transferrin (pdb code 2o84). 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 Crystal Structure of K206E Mutant of N-Lobe Human Transferrin, PDB code: 2o84:

Potassium binding site 1 out of 1 in the Crystal Structure of K206E Mutant of N-Lobe Human Transferrin


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of K206E Mutant of N-Lobe Human Transferrin within 5.0Å range: probe atom residue distance (Å) B Occ X:K601 b:22.9 occ:1.00 OE1 X:GLN169 2.8 15.3 1.0 O X:PHE154 2.8 14.1 1.0 O X:ALA151 3.1 14.5 1.0 O X:ASN152 3.4 13.9 1.0 C X:ASN152 3.9 13.8 1.0 CA X:ASN152 3.9 14.1 1.0 CD X:GLN169 4.0 15.7 1.0 C X:PHE154 4.0 13.6 1.0 C X:ALA151 4.2 14.1 1.0 CA X:SER155 4.2 13.8 1.0 N X:ASN152 4.5 14.0 1.0 N X:SER155 4.6 13.8 1.0 CG X:GLN169 4.6 16.8 1.0 O X:HOH650 4.7 2.0 1.0 C X:SER155 4.9 14.2 1.0 N X:PHE153 4.9 13.5 1.0 N X:GLY156 4.9 14.1 1.0 N X:PHE154 5.0 12.9 1.0 NE2 X:GLN169 5.0 15.6 1.0

H.M.Baker, D.Nurizzo, A.B.Mason, E.N.Baker. Structures of Two Mutants That Probe the Role in Iron Release of the Dilysine Pair in the N-Lobe of Human Transferrin. Acta Crystallogr.,Sect.D V. 63 408 2007.
ISSN: ISSN 0907-4449
PubMed: 17327678
DOI: 10.1107/S0907444907000182