Chlorine in PDB 8tsf: Pseudomonas Fluorescens G150T Isocyanide Hydratase at 298 K Xfel Data, Free Enzyme

The structure of Pseudomonas Fluorescens G150T Isocyanide Hydratase at 298 K Xfel Data, Free Enzyme, PDB code: 8tsf 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)	22.00 / 1.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	72.129, 59.855, 56.143, 90, 115.89, 90
R / Rfree (%)	14.3 / 17.1

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

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


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, Free Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:27.6 occ:1.00 HG1 A:THR153 2.2 20.7 0.3 H A:THR153 2.2 12.2 0.3 HH21 A:ARG139 2.3 31.0 0.6 HA3 A:GLY151 2.8 14.5 0.3 HG1 A:THR153 2.8 15.0 0.7 HA3 A:GLY151 2.9 14.3 0.7 H A:THR153 2.9 10.6 0.7 OG1 A:THR153 2.9 12.5 0.7 H A:ILE152 3.0 14.7 0.3 OG1 A:THR153 3.0 17.2 0.3 N A:THR153 3.1 10.2 0.3 HE A:ARG139 3.1 25.5 0.6 NH2 A:ARG139 3.1 25.8 0.6 N A:ILE152 3.2 12.2 0.3 C A:GLY151 3.4 11.9 0.3 CA A:GLY151 3.5 12.1 0.3 HG23 A:THR153 3.5 17.7 0.3 H A:ALA154 3.6 14.7 0.3 HH22 A:ARG139 3.7 31.0 0.6 CA A:GLY151 3.7 11.9 0.7 N A:THR153 3.7 8.8 0.7 HA2 A:GLY151 3.7 14.5 0.3 NE A:ARG139 3.8 21.2 0.6 CA A:THR153 3.8 12.1 0.3 CB A:THR153 3.8 14.9 0.3 CZ A:ARG139 4.0 22.5 0.6 HG13 A:ILE152 4.0 15.4 0.3 C A:GLY151 4.0 10.2 0.7 N A:ALA154 4.0 12.2 0.3 HG12 A:ILE152 4.0 15.4 0.3 C A:ILE152 4.0 13.2 0.3 HA2 A:GLY151 4.0 14.3 0.7 H A:ILE152 4.0 11.9 0.7 O A:HOH518 4.1 20.9 1.0 H A:ALA154 4.1 10.1 0.7 CB A:THR153 4.1 11.2 0.7 N A:ILE152 4.1 9.9 0.7 CG2 A:THR153 4.1 14.7 0.3 CA A:ILE152 4.1 13.2 0.3 CA A:THR153 4.2 9.6 0.7 O A:GLY151 4.2 11.5 0.3 N A:ALA154 4.2 8.4 0.7 C A:THR153 4.2 9.0 0.7 C A:THR153 4.2 11.8 0.3 O A:THR150 4.3 16.1 1.0 HG22 A:ILE152 4.3 12.6 0.7 CG1 A:ILE152 4.4 12.9 0.3 O A:GLY151 4.6 10.7 0.7 HG21 A:THR153 4.6 17.7 0.3 HG23 A:THR153 4.6 15.8 0.7 HA A:ALA154 4.6 11.7 0.7 HA A:THR153 4.7 14.6 0.3 N A:GLY151 4.7 11.2 0.3 HB A:THR153 4.7 17.9 0.3 HB2 A:ALA154 4.7 10.8 0.3 HB A:THR153 4.8 13.4 0.7 N A:GLY151 4.8 12.7 0.7 O A:THR153 4.8 9.1 0.7 C A:ILE152 4.8 9.0 0.7 HA A:ILE152 4.9 15.8 0.3 HG22 A:THR153 4.9 17.7 0.3 CG2 A:THR153 4.9 13.1 0.7 CB A:ILE152 5.0 12.5 0.3 C A:THR150 5.0 13.1 1.0 CA A:ALA154 5.0 9.8 0.7 HG23 A:ILE152 5.0 12.6 0.7

N.Smith, M.Dasgupta, D.C.Wych, C.Dolamore, R.G.Sierra, S.Lisova, D.Marchany-Rivera, A.E.Cohen, S.Boutet, M.S.Hunter, C.Kupitz, F.Poitevin, F.R.Moss, 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. Biorxiv 2023.
ISSN: ISSN 2692-8205
PubMed: 37645800
DOI: 10.1101/2023.08.15.553460