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Chlorine in PDB 5k3f: Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand

Enzymatic activity of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand

All present enzymatic activity of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand:
3.8.1.3;

Protein crystallography data

The structure of Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand, PDB code: 5k3f 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) 36.81 / 1.54
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.830, 79.620, 85.230, 90.00, 103.09, 90.00
R / Rfree (%) 17.9 / 22.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand (pdb code 5k3f). 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 Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand, PDB code: 5k3f:

Chlorine binding site 1 out of 1 in 5k3f

Go back to Chlorine Binding Sites List in 5k3f
Chlorine binding site 1 out of 1 in the Crystal Structure of the Fluoroacetate Dehalogenase RPA1163 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand


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 - HIS280ASN/Fluoroacetate - Cocrystallized - Single Protomer Reacted with Ligand within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl401

b:23.1
occ:1.00
 OD1 B:ASP110 2.9 18.6 1.0
NE B:ARG114 3.0 9.5 1.0
O B:HOH503 3.1 26.5 1.0
CG B:ASP110 3.3 10.2 1.0
NH1 B:ARG114 3.4 8.2 1.0
NH1 B:ARG111 3.4 8.3 1.0
OD2 B:ASP110 3.5 8.8 1.0
CD B:ARG111 3.6 7.6 1.0
O B:HOH523 3.6 19.9 1.0
O B:HOH689 3.6 15.6 1.0
CZ B:ARG114 3.6 6.2 1.0
O B:HOH518 3.7 22.8 1.0
C B:ASP110 4.0 7.0 1.0
N B:ARG111 4.0 7.3 1.0
CD B:ARG114 4.1 5.8 1.0
CA B:ASP110 4.1 9.1 1.0
CZ2 B:TRP156 4.2 9.7 1.0
CB B:ASP110 4.3 11.2 1.0
CZ B:ARG111 4.4 6.9 1.0
OH B:TYR219 4.4 21.4 1.0
NE B:ARG111 4.4 9.3 1.0
NE1 B:TRP156 4.6 9.4 1.0
O B:ASP110 4.6 6.8 1.0
CA B:ARG111 4.6 6.5 1.0
CG2 B:ILE135 4.7 12.1 1.0
CG B:ARG111 4.7 7.4 1.0
CE2 B:TRP156 4.7 7.1 1.0
CG B:ARG114 4.9 7.7 1.0
NH2 B:ARG114 5.0 7.5 1.0

Reference:

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
Page generated: Fri Jul 26 10:25:17 2024

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