Chlorine in PDB 8vq1: Pseudomonas Fluorescens G150T Isocyanide Hydratase at 298 K Xfel Data, Thioimidate Intermediate

The structure of Pseudomonas Fluorescens G150T Isocyanide Hydratase at 298 K Xfel Data, Thioimidate Intermediate, PDB code: 8vq1 was solved by M.A.Wilson, N.Smith, M.Dasgupta, C.Dolamore, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.98 / 1.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	72.136, 59.758, 56.11, 90, 115.88, 90
R / Rfree (%)	13.7 / 17.1

The binding sites of Chlorine atom in the Pseudomonas Fluorescens G150T Isocyanide Hydratase at 298 K Xfel Data, Thioimidate Intermediate (pdb code 8vq1). 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 Pseudomonas Fluorescens G150T Isocyanide Hydratase at 298 K Xfel Data, Thioimidate Intermediate, PDB code: 8vq1:

Chlorine binding site 1 out of 1 in the Pseudomonas Fluorescens G150T Isocyanide Hydratase at 298 K Xfel Data, Thioimidate Intermediate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Pseudomonas Fluorescens G150T Isocyanide Hydratase at 298 K Xfel Data, Thioimidate Intermediate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:26.1 occ:1.00 HG1 A:THR153 2.2 22.9 0.6 HH21 A:ARG139 2.2 35.8 0.7 H A:THR153 2.4 15.5 0.6 HG1 A:THR153 2.7 19.0 0.4 HA3 A:GLY151 2.9 18.9 0.4 HA3 A:GLY151 2.9 18.4 0.6 HE A:ARG139 3.0 32.7 0.7 OG1 A:THR153 3.0 15.8 0.4 OG1 A:THR153 3.0 19.1 0.6 NH2 A:ARG139 3.1 29.8 0.7 N A:THR153 3.2 12.9 0.6 H A:ILE152 3.2 16.3 0.6 H A:THR153 3.3 16.3 0.4 N A:ILE152 3.5 13.6 0.6 HG23 A:THR153 3.6 22.0 0.6 C A:GLY151 3.6 15.1 0.6 HH22 A:ARG139 3.7 35.8 0.7 CA A:GLY151 3.7 15.3 0.6 NE A:ARG139 3.7 27.3 0.7 CA A:GLY151 3.7 15.8 0.4 H A:ALA154 3.8 19.7 0.6 CB A:THR153 3.8 16.4 0.6 CZ A:ARG139 3.8 29.0 0.7 HA2 A:GLY151 3.9 18.9 0.4 CA A:THR153 3.9 14.8 0.6 O A:HOH513 4.0 24.5 1.0 HA2 A:GLY151 4.0 18.4 0.6 HG13 A:ILE152 4.1 20.8 0.6 N A:ALA154 4.1 16.4 0.6 N A:THR153 4.1 13.6 0.4 C A:GLY151 4.1 15.3 0.4 CG2 A:THR153 4.2 18.3 0.6 C A:ILE152 4.2 15.3 0.6 CB A:THR153 4.2 14.3 0.4 C A:THR153 4.3 16.9 0.6 HG12 A:ILE152 4.3 20.8 0.6 O A:GLY151 4.3 17.6 0.6 CA A:ILE152 4.4 15.2 0.6 H A:ALA154 4.4 12.8 0.4 C A:THR153 4.4 11.8 0.4 O A:THR150 4.4 18.8 1.0 N A:ALA154 4.4 10.7 0.4 CA A:THR153 4.5 13.0 0.4 H A:ILE152 4.5 17.7 0.4 N A:ILE152 4.5 14.7 0.4 HG21 A:THR153 4.6 22.0 0.6 CG1 A:ILE152 4.6 17.3 0.6 HA A:ALA154 4.6 12.8 0.4 O A:GLY151 4.7 16.4 0.4 HB A:THR153 4.7 19.7 0.6 HG22 A:ILE152 4.7 16.1 0.4 HB2 A:ALA154 4.7 24.1 0.6 HA A:THR153 4.8 17.8 0.6 HG23 A:THR153 4.8 18.2 0.4 HB A:THR153 4.8 17.1 0.4 N A:GLY151 4.8 13.0 0.6 N A:GLY151 4.9 14.4 0.4 O A:THR153 4.9 13.1 0.4 HG22 A:THR153 4.9 22.0 0.6 CD A:ARG139 5.0 25.0 0.7

N.Smith, M.Dasgupta, D.C.Wych, C.Dolamore, R.G.Sierra, S.Lisova, D.Rivera-Marchany, A.Cohen, S.Boutet, M.S.Hunter, C.Kupitz, F.Poitevin, F.R.Moss Iii, D.W.Mittan-Moreau, A.S.Brewster, N.K.Sauter, I.D.Young, A.M.Wolff, V.K.Tiwari, N.Kumar, D.B.Berkowitz, R.G.Hadt, M.C.Thompson, A.H.Follmer, M.E.Wall, M.A.Wilson. Changes in An Enzyme Ensemble During Catalysis Observed By High Resolution Xfel Crystallography Sci Adv 2024.
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