Chlorine in PDB 3viv: 1510-N Membrane-Bound Stomatin-Specific Protease K138A Mutant in Complex with A Substrate Peptide

The structure of 1510-N Membrane-Bound Stomatin-Specific Protease K138A Mutant in Complex with A Substrate Peptide, PDB code: 3viv was solved by H.Yokoyama, I.Matsui, S.Fujii, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.74 / 2.25
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	111.473, 111.473, 91.768, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 24.8

The binding sites of Chlorine atom in the 1510-N Membrane-Bound Stomatin-Specific Protease K138A Mutant in Complex with A Substrate Peptide (pdb code 3viv). 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 1510-N Membrane-Bound Stomatin-Specific Protease K138A Mutant in Complex with A Substrate Peptide, PDB code: 3viv:

Chlorine binding site 1 out of 1 in the 1510-N Membrane-Bound Stomatin-Specific Protease K138A Mutant in Complex with A Substrate Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of 1510-N Membrane-Bound Stomatin-Specific Protease K138A Mutant in Complex with A Substrate Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:21.7 occ:0.50 NH1 A:ARG208 3.1 42.6 1.0 N A:THR211 3.2 38.8 1.0 O A:HOH440 3.8 34.0 1.0 NH2 A:ARG208 3.9 42.2 1.0 CA A:VAL210 3.9 39.1 1.0 CB A:THR211 4.0 40.3 1.0 CZ A:ARG208 4.0 42.9 1.0 CA A:THR211 4.0 38.8 1.0 C A:VAL210 4.0 38.1 1.0 O A:THR211 4.1 39.1 1.0 CG2 A:VAL210 4.3 40.5 1.0 OG1 A:THR211 4.3 40.0 1.0 CB A:VAL210 4.5 39.0 1.0 C A:THR211 4.5 38.5 1.0 CG1 A:VAL210 4.8 40.6 1.0 O A:TYR209 4.8 42.1 1.0 O A:HOH421 5.0 35.4 1.0

H.Yokoyama, N.Takizawa, D.Kobayashi, I.Matsui, S.Fujii. Crystal Structure of A Membrane Stomatin-Specific Protease in Complex with A Substrate Peptide Biochemistry V. 51 3872 2012.
ISSN: ISSN 0006-2960
PubMed: 22475127
DOI: 10.1021/BI300098K