Chlorine in PDB 6p0m: Crystal Structure of Gdp-Bound Human Rala in A Covalent Complex with Aryl Sulfonyl Fluoride Compounds.

The structure of Crystal Structure of Gdp-Bound Human Rala in A Covalent Complex with Aryl Sulfonyl Fluoride Compounds., PDB code: 6p0m was solved by K.Bum-Erdene, G.Gonzalez-Gutierrez, D.Liu, M.K.Ghozayel, D.Xu, S.O.Meroueh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.15 / 1.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	65.095, 104.370, 55.489, 90.00, 90.00, 90.00
R / Rfree (%)	13.3 / 16.9

The structure of Crystal Structure of Gdp-Bound Human Rala in A Covalent Complex with Aryl Sulfonyl Fluoride Compounds. also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of Gdp-Bound Human Rala in A Covalent Complex with Aryl Sulfonyl Fluoride Compounds. (pdb code 6p0m). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Gdp-Bound Human Rala in A Covalent Complex with Aryl Sulfonyl Fluoride Compounds., PDB code: 6p0m:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Gdp-Bound Human Rala in A Covalent Complex with Aryl Sulfonyl Fluoride Compounds.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Gdp-Bound Human Rala in A Covalent Complex with Aryl Sulfonyl Fluoride Compounds. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl501 b:36.2 occ:1.00 CL1 B:NLM501 0.0 36.2 1.0 C18 B:NLM501 1.7 29.5 1.0 H121 B:NLM501 2.5 27.4 1.0 C13 B:NLM501 2.6 25.9 1.0 HA2 B:GLY71 2.6 25.4 1.0 C17 B:NLM501 2.7 26.1 1.0 H171 B:NLM501 2.8 31.3 1.0 N12 B:NLM501 2.8 22.8 1.0 H B:GLY71 3.0 23.2 1.0 CA B:GLY71 3.3 21.1 1.0 N B:GLY71 3.5 19.3 1.0 HB3 B:GLU73 3.6 33.3 1.0 H B:GLU73 3.6 31.6 1.0 HB B:THR69 3.7 11.5 1.0 C B:GLY71 3.8 23.1 1.0 O B:HOH791 3.8 20.9 1.0 N14 B:NLM501 3.9 26.2 1.0 C16 B:NLM501 3.9 25.4 1.0 H B:GLN72 4.1 29.6 1.0 HA3 B:GLY71 4.1 25.4 1.0 O B:GLU73 4.1 31.9 1.0 N B:GLN72 4.2 24.7 1.0 S09 B:NLM501 4.2 18.7 1.0 HG3 B:ARG79 4.2 12.0 1.0 O B:HOH669 4.2 10.7 1.0 N B:GLU73 4.3 26.3 1.0 O B:GLY71 4.3 24.2 1.0 C15 B:NLM501 4.3 27.2 1.0 HG2 B:ARG79 4.3 12.0 1.0 CB B:GLU73 4.4 27.8 1.0 O11 B:NLM501 4.5 16.9 1.0 H B:ALA70 4.5 15.9 1.0 CB B:THR69 4.6 9.6 1.0 O B:HOH684 4.6 16.3 1.0 H161 B:NLM501 4.7 30.5 1.0 HB2 B:GLU73 4.7 33.3 1.0 HG21 B:THR69 4.7 13.3 1.0 CG B:ARG79 4.7 10.0 1.0 CA B:GLU73 4.8 27.1 1.0 O10 B:NLM501 4.8 27.2 1.0 OG1 B:THR69 4.8 10.4 1.0 C B:GLU73 4.8 29.4 1.0 C B:ALA70 4.8 19.0 1.0 HE2 B:PHE107 4.9 10.6 1.0 N B:ALA70 5.0 13.3 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Gdp-Bound Human Rala in A Covalent Complex with Aryl Sulfonyl Fluoride Compounds.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Gdp-Bound Human Rala in A Covalent Complex with Aryl Sulfonyl Fluoride Compounds. within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl503 b:52.7 occ:1.00 HB2 B:SER50 3.0 25.4 1.0 HA B:ASP49 3.2 17.6 1.0 H B:SER50 3.2 17.8 1.0 OG B:SER50 3.3 28.2 1.0 N B:SER50 3.4 14.8 1.0 HG B:SER50 3.5 33.8 1.0 CB B:SER50 3.6 21.1 1.0 C B:ASP49 3.8 14.3 1.0 CA B:ASP49 3.9 14.7 1.0 HD13 B:LEU67 4.0 14.0 1.0 CA B:SER50 4.1 14.9 1.0 OD1 B:ASP49 4.2 18.2 1.0 O1 B:NLM501 4.3 33.6 1.0 HD11 B:LEU67 4.4 14.0 1.0 HD12 B:LEU67 4.4 14.0 1.0 HB3 B:SER50 4.5 25.4 1.0 CD1 B:LEU67 4.5 11.6 1.0 HA B:SER50 4.6 17.8 1.0 N B:ASP49 4.6 16.1 1.0 O B:ASP49 4.6 12.5 1.0 H061 B:NLM501 4.6 32.5 1.0 O B:ALA48 4.7 17.9 1.0 C B:ALA48 4.9 15.4 1.0 H B:ASP49 5.0 19.3 1.0

K.Bum-Erdene, D.Liu, G.Gonzalez-Gutierrez, M.K.Ghozayel, D.Xu, S.O.Meroueh. Small-Molecule Covalent Bond Formation at Tyrosine Creates A New Binding Site and Inhibits Activation of Ral Gtpases Proc.Natl.Acad.Sci.Usa 2020.
ISSN: ESSN 1091-6490
DOI: 10.1073/PNAS.1913654117