Chlorine in PDB 3ssh: Engineered High-Affinity Halide-Binding Protein Derived From Yfp: Chloride Complex

The structure of Engineered High-Affinity Halide-Binding Protein Derived From Yfp: Chloride Complex, PDB code: 3ssh was solved by W.Wang, J.S.Grimley, L.S.Beese, H.W.Hellinga, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.22 / 1.28
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.266, 62.405, 69.325, 90.00, 90.00, 90.00
R / Rfree (%)	13 / 16

The binding sites of Chlorine atom in the Engineered High-Affinity Halide-Binding Protein Derived From Yfp: Chloride Complex (pdb code 3ssh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Engineered High-Affinity Halide-Binding Protein Derived From Yfp: Chloride Complex, PDB code: 3ssh:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Engineered High-Affinity Halide-Binding Protein Derived From Yfp: Chloride Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Engineered High-Affinity Halide-Binding Protein Derived From Yfp: Chloride Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl260 b:12.5 occ:0.90 HE21 A:GLN69 2.4 17.6 1.0 HE A:ARG96 2.5 12.7 1.0 HH21 A:ARG96 2.5 14.9 1.0 HD21 A:ASN185 2.5 16.1 1.0 HG21 A:VAL163 3.0 16.7 1.0 HB A:VAL163 3.0 16.1 1.0 HG11 A:VAL163 3.1 18.6 1.0 HB3 A:ALA183 3.1 16.6 1.0 HB1 A:ALA183 3.2 16.6 1.0 HE22 A:GLN94 3.2 16.2 1.0 NH2 A:ARG96 3.2 12.6 1.0 NE A:ARG96 3.3 10.7 1.0 NE2 A:GLN69 3.3 14.8 1.0 ND2 A:ASN185 3.3 13.5 1.0 CB A:ALA183 3.5 13.9 1.0 HG3 A:GLN94 3.5 14.2 1.0 NE2 A:GLN94 3.6 13.6 1.0 CB A:VAL163 3.6 13.5 1.0 HB2 A:ALA183 3.6 16.6 1.0 CZ A:ARG96 3.7 9.9 1.0 CG2 A:VAL163 3.7 14.0 1.0 HD22 A:ASN185 3.7 16.1 1.0 CG1 A:VAL163 3.7 15.6 1.0 HE2 A:PHE165 3.7 14.5 1.0 OE1 A:GLN69 3.8 13.5 1.0 HE22 A:GLN69 3.8 17.6 1.0 HH22 A:ARG96 3.9 14.9 1.0 HE21 A:GLN94 3.9 16.2 1.0 CD A:GLN69 3.9 13.2 1.0 HG23 A:VAL163 4.0 16.7 1.0 HG12 A:VAL163 4.1 18.6 1.0 CD A:GLN94 4.2 12.3 1.0 CG A:GLN94 4.2 11.9 1.0 CG A:ASN185 4.3 13.2 1.0 HG2 A:ARG96 4.4 13.3 1.0 OD1 A:ASN185 4.4 13.8 1.0 CD A:ARG96 4.4 11.2 1.0 HG22 A:VAL163 4.5 16.7 1.0 HG13 A:VAL163 4.5 18.6 1.0 HD3 A:ARG96 4.6 13.3 1.0 HG2 A:GLN94 4.6 14.2 1.0 CE2 A:PHE165 4.6 12.2 1.0 O A:HOH480 4.7 25.1 1.0 HE2 A:PHE84 4.7 13.6 1.0 CG A:ARG96 4.9 11.2 1.0 CA A:ALA183 4.9 11.8 1.0 HG11 A:VAL150 4.9 19.1 1.0 NH1 A:ARG96 5.0 9.9 1.0

Chlorine binding site 2 out of 2 in the Engineered High-Affinity Halide-Binding Protein Derived From Yfp: Chloride Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Engineered High-Affinity Halide-Binding Protein Derived From Yfp: Chloride Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl261 b:11.3 occ:0.77 H A:TRP57 2.4 10.6 1.0 O A:HOH440 2.9 21.9 1.0 O A:HOH390 3.0 18.6 1.0 HA A:PRO56 3.0 10.3 1.0 O A:HOH357 3.1 14.7 1.0 HB2 A:TRP57 3.1 10.0 1.0 HD3 A:PRO58 3.1 10.2 1.0 N A:TRP57 3.2 8.9 1.0 HD1 A:TYR143 3.2 12.6 1.0 O A:HOH410 3.2 22.9 1.0 HD2 A:PRO58 3.5 10.2 1.0 HB3 A:PRO56 3.5 11.7 1.0 CD1 A:TRP57 3.7 9.3 1.0 CA A:PRO56 3.7 8.7 1.0 CD A:PRO58 3.7 8.6 1.0 CB A:TRP57 3.8 8.5 1.0 C A:PRO56 3.9 8.2 1.0 CD1 A:TYR143 4.0 10.6 1.0 CA A:TRP57 4.1 8.0 1.0 CB A:PRO56 4.1 9.9 1.0 CG A:TRP57 4.1 8.0 1.0 HE1 A:TYR143 4.2 12.0 1.0 HD1 A:HIS139 4.4 19.2 1.0 O A:HOH351 4.4 13.1 1.0 O A:HOH425 4.4 28.6 1.0 CE1 A:TYR143 4.5 10.1 1.0 HB2 A:TYR143 4.5 11.8 1.0 HZ3 A:LYS209 4.6 13.4 1.0 HB2 A:PRO56 4.6 11.7 1.0 O A:HOH436 4.7 35.8 1.0 HB3 A:TRP57 4.7 10.0 1.0 O A:HOH457 4.7 38.2 1.0 N A:PRO58 4.7 7.7 1.0 HA A:TRP57 4.8 9.4 1.0 HG2 A:PRO58 4.8 10.8 1.0 CG A:PRO58 4.8 9.1 1.0 NE1 A:TRP57 4.9 9.4 1.0 O A:HOH526 5.0 28.4 1.0 C A:TRP57 5.0 8.0 1.0 HA A:TYR143 5.0 10.9 1.0

W.Wang, J.S.Grimley, G.J.Augustine, L.S.Beese, H.W.Hellinga. Determination of Engineered Chloride-Binding Site Structures in Fluorescent Proteins Reveals Principles of Halide Recognition To Be Published.