Chlorine in PDB 3hda: Prtc Methionine Mutants: M226A_DESY

The structure of Prtc Methionine Mutants: M226A_DESY, PDB code: 3hda was solved by A.E.Oberholzer, M.Bumann, T.Hege, S.Russo, U.Baumann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.51 / 2.13
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	101.858, 101.858, 122.521, 90.00, 90.00, 120.00
R / Rfree (%)	18.2 / 20.7

The structure of Prtc Methionine Mutants: M226A_DESY also contains other interesting chemical elements:

Calcium

(Ca)

7 atoms

The binding sites of Chlorine atom in the Prtc Methionine Mutants: M226A_DESY (pdb code 3hda). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Prtc Methionine Mutants: M226A_DESY, PDB code: 3hda:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Prtc Methionine Mutants: M226A_DESY


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Prtc Methionine Mutants: M226A_DESY within 5.0Å range: probe atom residue distance (Å) B Occ P:Cl1 b:37.9 occ:1.00 O P:HOH659 3.0 49.8 1.0 OG P:SER269 3.0 21.6 1.0 O P:HOH562 3.1 36.0 1.0 N P:GLY267 3.5 22.0 1.0 C P:GLY267 3.6 27.6 1.0 CA P:GLY267 3.6 24.0 1.0 CA P:ARG265 3.7 25.9 1.0 O P:GLY267 3.7 26.2 1.0 C P:ARG265 3.8 24.4 1.0 CB P:ARG265 4.0 25.9 1.0 CB P:SER269 4.1 19.2 1.0 O P:ARG265 4.1 22.7 1.0 N P:THR266 4.2 20.6 1.0 N P:ASP268 4.3 25.4 1.0 C P:ASP268 4.3 23.8 1.0 CA P:SER269 4.3 21.9 1.0 O P:ASP268 4.3 23.4 1.0 CG P:ARG265 4.4 27.1 1.0 N P:SER269 4.4 22.7 1.0 CA P:CA480 4.5 23.5 1.0 C P:THR266 4.6 23.9 1.0 O P:HOH653 4.8 31.8 1.0 CA P:ASP268 4.9 24.4 1.0 N P:ARG265 5.0 23.1 1.0

Chlorine binding site 2 out of 2 in the Prtc Methionine Mutants: M226A_DESY


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Prtc Methionine Mutants: M226A_DESY within 5.0Å range: probe atom residue distance (Å) B Occ P:Cl3 b:48.4 occ:1.00 O P:HOH508 2.9 33.2 1.0 O P:HOH694 3.0 42.3 1.0 OG P:SER113 3.0 27.1 1.0 CA P:GLN110 3.7 27.0 1.0 CD1 P:PHE120 3.8 23.6 1.0 N P:GLN110 3.9 23.4 1.0 CB P:SER113 3.9 27.4 1.0 CB P:PHE120 4.1 29.5 1.0 C P:LEU109 4.2 27.5 1.0 CB P:GLN110 4.2 26.5 1.0 O P:LEU109 4.2 27.9 1.0 O P:HOH6 4.4 27.9 1.0 CG P:PHE120 4.5 23.8 1.0 CB P:LEU109 4.6 20.5 1.0 O P:HOH605 4.6 48.5 1.0 N P:PHE120 4.7 31.2 1.0 CE1 P:PHE120 4.8 24.6 1.0 CG P:GLN110 4.9 28.9 1.0 O P:PHE120 4.9 33.6 1.0 C P:GLN110 4.9 27.0 1.0 CA P:PHE120 5.0 31.9 1.0

A.E.Oberholzer, M.Bumann, T.Hege, S.Russo, U.Baumann. Metzincin'S Canonical Methionine Is Responsible For the Structural Integrity of the Zinc-Binding Site Biol.Chem. V. 390 875 2009.
ISSN: ISSN 1431-6730
PubMed: 19558324
DOI: 10.1515/BC.2009.100