Chlorine in PDB 6xu9: Human Myelin Protein P2 Mutant K3N

The structure of Human Myelin Protein P2 Mutant K3N, PDB code: 6xu9 was solved by S.Ruskamo, M.Lehtimaki, P.Kursula, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.70
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	64.520, 64.520, 101.210, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 25

The binding sites of Chlorine atom in the Human Myelin Protein P2 Mutant K3N (pdb code 6xu9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Human Myelin Protein P2 Mutant K3N, PDB code: 6xu9:

Chlorine binding site 1 out of 1 in the Human Myelin Protein P2 Mutant K3N


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Myelin Protein P2 Mutant K3N within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:46.3 occ:1.00 H A:LYS37 2.5 46.0 1.0 H A:THR56 2.8 42.4 1.0 HB2 A:SER55 3.2 39.9 1.0 N A:LYS37 3.3 38.3 1.0 HA A:ALA36 3.4 43.6 1.0 HA A:SER55 3.5 39.4 1.0 O A:HOH332 3.6 32.3 1.0 N A:THR56 3.7 35.3 1.0 O A:LYS37 3.7 39.7 1.0 HB2 A:LYS37 3.8 52.8 1.0 C A:LYS37 3.9 36.6 1.0 HB A:THR56 3.9 40.7 1.0 OG1 A:THR56 4.0 39.9 1.0 CB A:SER55 4.0 33.2 1.0 HB1 A:ALA36 4.0 42.0 1.0 CA A:LYS37 4.1 39.8 1.0 CA A:SER55 4.1 32.9 1.0 CA A:ALA36 4.1 36.4 1.0 HG1 A:THR56 4.1 47.9 1.0 C A:ALA36 4.2 38.3 1.0 HA A:PRO38 4.2 39.4 1.0 HB3 A:SER55 4.3 39.9 1.0 CB A:THR56 4.4 33.9 1.0 CB A:LYS37 4.4 44.0 1.0 C A:SER55 4.4 34.6 1.0 N A:PRO38 4.5 33.5 1.0 CB A:ALA36 4.5 35.0 1.0 CA A:THR56 4.7 33.4 1.0 H A:PHE57 4.7 40.3 1.0 HB2 A:ALA36 4.8 42.0 1.0 HB3 A:LYS37 4.9 52.8 1.0 CA A:PRO38 4.9 32.8 1.0 HA A:LYS37 4.9 47.8 1.0

S.Ruskamo, O.C.Krokengen, J.Kowal, T.Nieminen, M.Lehtimaki, A.Raassakka, S.Laulumaa, B.P.Dandey, I.Vattulainen, H.Stahlberg, P.Kursula. Human Myelin Protein P2: Determinants For Forming A Supramolecular Proteolipid Lattice To Be Published.