Chlorine in PDB 5k3c: Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Wt/5- Fluorotryptophan

All present enzymatic activity of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Wt/5- Fluorotryptophan:
3.8.1.3;

The structure of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Wt/5- Fluorotryptophan, PDB code: 5k3c was solved by P.Mehrabi, T.H.Kim, S.R.Prosser, E.F.Pai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.14 / 1.54
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.890, 79.460, 85.240, 90.00, 103.02, 90.00
R / Rfree (%)	17.4 / 21.1

The structure of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Wt/5- Fluorotryptophan also contains other interesting chemical elements:

Fluorine

(F)

18 atoms

The binding sites of Chlorine atom in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Wt/5- Fluorotryptophan (pdb code 5k3c). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Wt/5- Fluorotryptophan, PDB code: 5k3c:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Wt/5- Fluorotryptophan


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Wt/5- Fluorotryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:19.2 occ:1.00 O A:HOH585 3.0 20.4 1.0 NH1 A:ARG114 3.0 8.8 1.0 N A:LEU136 3.1 10.5 1.0 O A:LEU136 3.7 8.4 1.0 CA A:ILE135 3.8 6.3 1.0 C A:ILE135 3.9 8.1 1.0 CA A:LEU136 4.0 8.4 1.0 CB A:LEU136 4.0 12.8 1.0 CZ A:ARG114 4.2 6.2 1.0 C A:LEU136 4.3 8.4 1.0 CB A:ILE135 4.3 6.8 1.0 CG A:LEU136 4.4 13.0 1.0 NH2 A:ARG114 4.5 8.9 1.0 CZ2 A:FTR156 4.7 10.9 1.0 O A:ASP134 4.7 10.8 1.0 CB A:TYR141 4.8 12.5 1.0 CG2 A:ILE135 4.8 8.2 1.0 CH2 A:FTR156 4.9 9.9 1.0 CD2 A:TYR141 4.9 26.7 1.0 CG1 A:ILE253 4.9 31.2 1.0 CD1 A:LEU136 5.0 20.9 1.0 N A:ILE135 5.0 7.7 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Wt/5- Fluorotryptophan


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Wt/5- Fluorotryptophan within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:14.2 occ:1.00 NE A:ARG114 3.0 7.8 1.0 O A:HOH515 3.2 24.4 1.0 NH1 A:ARG114 3.3 8.8 1.0 O A:HOH718 3.3 19.3 1.0 OD1 A:ASP110 3.3 12.5 1.0 NH1 A:ARG111 3.4 9.2 1.0 CG A:ASP110 3.5 8.1 1.0 OD2 A:ASP110 3.6 7.1 1.0 CZ A:ARG114 3.6 6.2 1.0 CD A:ARG111 3.7 8.6 1.0 C A:ASP110 4.0 5.7 1.0 N A:ARG111 4.0 6.5 1.0 CZ2 A:FTR156 4.1 10.9 1.0 CA A:ASP110 4.1 6.2 1.0 CD A:ARG114 4.1 7.0 1.0 CZ A:ARG111 4.4 9.7 1.0 CB A:ASP110 4.4 6.4 1.0 NE A:ARG111 4.4 8.4 1.0 O A:ASP110 4.4 6.6 1.0 CG2 A:ILE135 4.5 8.2 1.0 O A:HOH585 4.6 20.4 1.0 OH A:TYR219 4.6 15.2 1.0 CA A:ARG111 4.6 7.6 1.0 O A:HOH722 4.7 23.1 1.0 CE2 A:FTR156 4.7 10.5 1.0 CG A:ARG114 4.8 7.2 1.0 NE1 A:FTR156 4.8 11.3 1.0 CG A:ARG111 4.8 6.7 1.0 CH2 A:FTR156 4.8 9.9 1.0 O A:HOH518 4.8 18.4 1.0 NH2 A:ARG114 4.9 8.9 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Wt/5- Fluorotryptophan


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - Wt/5- Fluorotryptophan within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl401 b:17.0 occ:1.00 NE B:ARG114 3.0 10.7 1.0 O B:HOH509 3.3 20.4 1.0 O B:HOH635 3.3 27.4 1.0 OD1 B:ASP110 3.4 13.3 1.0 NH1 B:ARG114 3.4 12.4 1.0 CG B:ASP110 3.4 10.1 1.0 NH1 B:ARG111 3.4 9.4 1.0 OD2 B:ASP110 3.5 10.3 1.0 CZ B:ARG114 3.7 9.0 1.0 CD B:ARG111 3.7 10.1 1.0 C B:ASP110 3.8 8.9 1.0 N B:ARG111 3.8 9.0 1.0 CA B:ASP110 3.9 9.8 1.0 O B:HOH644 4.1 27.1 1.0 CD B:ARG114 4.1 11.1 1.0 CZ2 B:FTR156 4.1 12.4 1.0 CB B:ASP110 4.3 10.7 1.0 O B:ASP110 4.3 8.7 1.0 CG2 B:ILE135 4.4 12.7 1.0 CZ B:ARG111 4.4 9.5 1.0 CA B:ARG111 4.5 9.4 1.0 NE B:ARG111 4.5 10.5 1.0 O B:HOH504 4.6 26.0 1.0 CG B:ARG114 4.7 9.5 1.0 OH B:TYR219 4.8 14.8 1.0 CE2 B:FTR156 4.8 12.8 1.0 NE1 B:FTR156 4.8 14.2 1.0 CG B:ARG111 4.8 9.6 1.0 O B:HOH505 4.8 23.7 1.0 CH2 B:FTR156 4.9 12.5 1.0 NH2 B:ARG114 5.0 9.4 1.0

T.H.Kim, P.Mehrabi, Z.Ren, A.Sljoka, C.Ing, A.Bezginov, L.Ye, R.Pomes, R.S.Prosser, E.F.Pai. The Role of Dimer Asymmetry and Protomer Dynamics in Enzyme Catalysis. Science V. 355 2017.
ISSN: ESSN 1095-9203
PubMed: 28104837
DOI: 10.1126/SCIENCE.AAG2355