Chlorine in PDB 5k3b: Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Chloroacetate - Cocrystallized

All present enzymatic activity of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Chloroacetate - Cocrystallized:
3.8.1.3;

The structure of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Chloroacetate - Cocrystallized, PDB code: 5k3b 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)	18.79 / 1.58
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.837, 78.956, 84.986, 90.00, 103.28, 90.00
R / Rfree (%)	16.4 / 19.6

The binding sites of Chlorine atom in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Chloroacetate - Cocrystallized (pdb code 5k3b). 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 - ASP110ASN/Chloroacetate - Cocrystallized, PDB code: 5k3b:
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 - ASP110ASN/Chloroacetate - Cocrystallized


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 - ASP110ASN/Chloroacetate - Cocrystallized within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:17.4 occ:1.00 O A:HOH651 2.9 19.1 1.0 N A:LEU136 3.1 10.0 1.0 NH1 A:ARG114 3.1 10.4 1.0 O A:LEU136 3.7 8.7 1.0 CA A:ILE135 3.8 8.8 1.0 C A:ILE135 3.9 11.7 1.0 CB A:LEU136 3.9 10.4 1.0 CA A:LEU136 3.9 12.2 1.0 CA A:ALA254 4.1 29.6 1.0 CZ A:ARG114 4.2 6.7 1.0 CG A:LEU136 4.2 11.4 1.0 C A:LEU136 4.3 10.0 1.0 CB A:ILE135 4.3 6.4 1.0 CB A:ALA254 4.4 21.6 1.0 NH2 A:ARG114 4.4 8.3 1.0 CG2 A:ILE253 4.5 29.6 1.0 N A:ALA254 4.6 30.4 1.0 CB A:TYR141 4.7 16.5 1.0 CZ2 A:TRP156 4.7 15.7 1.0 O A:ASP134 4.8 9.8 1.0 CD2 A:TYR141 4.8 22.2 1.0 CG2 A:ILE135 4.8 9.6 1.0 CD1 A:LEU136 4.9 17.3 1.0 O A:ILE253 4.9 32.4 1.0 C A:ILE253 4.9 32.0 1.0 NH2 A:ARG144 4.9 42.0 1.0 N A:ILE135 5.0 10.7 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Chloroacetate - Cocrystallized


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 - ASP110ASN/Chloroacetate - Cocrystallized within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:26.1 occ:1.00 CL1 A:R3W402 0.0 26.1 1.0 C2 A:R3W402 1.8 21.0 1.0 C1 A:R3W402 2.6 14.9 1.0 O2 A:R3W402 2.7 28.3 1.0 NE2 A:HIS155 3.1 17.0 1.0 ND2 A:ASN110 3.4 10.3 1.0 OH A:TYR219 3.5 11.0 1.0 CH2 A:TRP185 3.5 12.7 1.0 CE1 A:HIS155 3.6 18.2 1.0 CD1 A:ILE253 3.6 20.6 1.0 O1 A:R3W402 3.7 4.9 1.0 CZ3 A:TRP185 3.8 14.1 1.0 NE1 A:TRP156 4.0 17.1 1.0 CZ2 A:TRP185 4.1 12.7 1.0 CG A:ASN110 4.3 9.4 1.0 CD2 A:HIS155 4.3 16.5 1.0 OD1 A:ASN110 4.5 8.2 1.0 CE3 A:TRP185 4.6 13.2 1.0 CZ A:TYR219 4.6 12.0 1.0 NE2 A:HIS280 4.6 11.0 1.0 CE2 A:TRP185 4.8 13.7 1.0 CD1 A:TRP156 4.8 14.1 1.0 CE1 A:TYR219 4.9 12.1 1.0 ND1 A:HIS155 4.9 19.8 1.0 CE2 A:TRP156 4.9 13.1 1.0 CE1 A:HIS280 5.0 12.5 1.0 O A:HOH651 5.0 19.1 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - ASP110ASN/Chloroacetate - Cocrystallized


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 - ASP110ASN/Chloroacetate - Cocrystallized within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl401 b:17.0 occ:1.00 NE B:ARG114 3.0 11.2 1.0 O B:HOH579 3.1 14.2 1.0 NH1 B:ARG114 3.4 12.2 1.0 CG B:ASN110 3.4 10.2 1.0 OD1 B:ASN110 3.5 9.9 1.0 C B:ASN110 3.5 8.7 1.0 NH1 B:ARG111 3.6 9.4 1.0 CA B:ASN110 3.6 10.3 1.0 ND2 B:ASN110 3.6 12.1 1.0 CZ B:ARG114 3.7 9.3 1.0 N B:ARG111 3.7 8.5 1.0 CD B:ARG111 3.7 10.1 1.0 CD B:ARG114 4.0 10.7 1.0 O B:ASN110 4.0 8.4 1.0 CB B:ASN110 4.1 10.8 1.0 CZ2 B:TRP156 4.3 10.9 1.0 CG2 B:ILE135 4.3 16.0 1.0 CA B:ARG111 4.4 8.7 1.0 CZ B:ARG111 4.5 9.6 1.0 NE B:ARG111 4.5 9.3 1.0 CG B:ARG114 4.6 8.1 1.0 O B:HOH503 4.7 20.3 1.0 CG B:ARG111 4.8 10.6 1.0 NE1 B:TRP156 4.8 12.0 1.0 OH B:TYR219 4.8 14.3 1.0 N B:ASN110 4.9 9.2 1.0 CE2 B:TRP156 4.9 10.8 1.0 NH2 B:ARG114 5.0 9.5 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