Chlorine in PDB 5ksp: HMIRO1 C-Domain Gdp Complex C2221 Crystal Form

The structure of HMIRO1 C-Domain Gdp Complex C2221 Crystal Form, PDB code: 5ksp was solved by J.L.Klosowiak, P.J.Focia, S.E.Rice, D.M.Freymann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.88 / 2.16
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	66.070, 72.640, 151.760, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 24.1

The binding sites of Chlorine atom in the HMIRO1 C-Domain Gdp Complex C2221 Crystal Form (pdb code 5ksp). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the HMIRO1 C-Domain Gdp Complex C2221 Crystal Form, PDB code: 5ksp:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the HMIRO1 C-Domain Gdp Complex C2221 Crystal Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of HMIRO1 C-Domain Gdp Complex C2221 Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl702 b:25.2 occ:1.00 O A:HOH805 3.1 32.5 1.0 NZ A:LYS431 3.2 20.0 1.0 N A:GLU478 3.2 14.1 1.0 O A:HOH856 3.2 29.9 1.0 CE A:LYS431 3.6 19.1 1.0 CA A:SER477 3.6 12.9 1.0 CD A:LYS427 3.7 42.3 1.0 CA A:LYS427 3.9 25.7 1.0 C A:SER477 4.0 17.4 1.0 CB A:SER477 4.0 19.3 1.0 CB A:GLU478 4.1 15.2 1.0 N A:LYS427 4.2 23.0 1.0 CA A:GLU478 4.3 20.9 1.0 CB A:LYS427 4.3 32.1 1.0 OG A:SER477 4.3 19.4 1.0 O A:VAL426 4.4 21.1 1.0 O A:HOH899 4.5 42.4 1.0 C A:VAL426 4.5 22.6 1.0 CG A:LYS427 4.6 34.0 1.0 O A:GLY425 4.6 15.5 1.0 O2B A:GDP701 4.6 24.3 1.0 CE A:LYS427 4.8 39.5 1.0 O A:ILE476 4.8 18.8 1.0 N A:SER477 4.8 11.9 1.0 O A:HOH834 4.9 29.9 1.0 O3B A:GDP701 4.9 31.7 1.0

Chlorine binding site 2 out of 2 in the HMIRO1 C-Domain Gdp Complex C2221 Crystal Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of HMIRO1 C-Domain Gdp Complex C2221 Crystal Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl702 b:27.1 occ:1.00 N B:GLU478 3.2 19.8 1.0 NZ B:LYS431 3.2 20.5 1.0 O B:HOH873 3.4 30.1 1.0 CG B:LYS427 3.6 31.9 1.0 CA B:SER477 3.6 18.8 1.0 CE B:LYS431 3.7 21.5 1.0 CA B:LYS427 3.8 29.5 1.0 CE A:MET516 3.9 29.2 1.0 C B:SER477 3.9 21.3 1.0 CB B:GLU478 4.0 19.7 1.0 N B:LYS427 4.1 21.0 1.0 CB B:SER477 4.1 18.0 1.0 CB B:LYS427 4.2 30.0 1.0 CA B:GLU478 4.2 19.9 1.0 O B:GLY425 4.4 17.4 1.0 C B:VAL426 4.4 19.8 1.0 O B:VAL426 4.4 18.2 1.0 OG B:SER477 4.5 24.7 1.0 O3B B:GDP701 4.6 33.7 1.0 SD A:MET516 4.6 29.9 1.0 O B:ILE476 4.6 18.3 1.0 CD B:LYS427 4.7 37.7 1.0 N B:SER477 4.8 19.2 1.0 O B:HOH829 4.8 38.7 1.0

J.L.Klosowiak, S.Park, K.P.Smith, M.E.French, P.J.Focia, D.M.Freymann, S.E.Rice. Structural Insights Into Parkin Substrate Lysine Targeting From Minimal Miro Substrates. Sci Rep V. 6 33019 2016.
ISSN: ESSN 2045-2322
PubMed: 27605430
DOI: 10.1038/SREP33019