Chlorine in PDB 7pf8: Synftn Variant E141A

All present enzymatic activity of Synftn Variant E141A:
1.16.3.2;

The structure of Synftn Variant E141A, PDB code: 7pf8 was solved by A.M.Hemmings, J.M.Bradley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.57 / 1.85
Space group	F 4 3 2
Cell size a, b, c (Å), α, β, γ (°)	176.85, 176.85, 176.85, 90, 90, 90
R / Rfree (%)	19.3 / 21.6

The structure of Synftn Variant E141A also contains other interesting chemical elements:

Sodium

(Na)

4 atoms

The binding sites of Chlorine atom in the Synftn Variant E141A (pdb code 7pf8). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Synftn Variant E141A, PDB code: 7pf8:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Synftn Variant E141A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Synftn Variant E141A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl205 b:61.1 occ:1.00 O A:HOH464 3.4 42.5 1.0 NH1 A:ARG93 3.4 35.2 1.0 CD A:ARG93 3.7 32.8 1.0 CG2 A:THR105 3.8 35.9 1.0 OG1 A:THR105 4.3 36.4 1.0 CZ A:ARG93 4.4 33.6 1.0 NE A:ARG93 4.5 33.7 1.0 CB A:THR105 4.7 33.1 1.0 CB A:ARG93 4.9 36.9 1.0 CG A:ARG93 4.9 35.3 1.0

Chlorine binding site 2 out of 2 in the Synftn Variant E141A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Synftn Variant E141A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl206 b:40.0 occ:1.00 O A:HOH456 3.0 44.6 1.0 O A:HOH319 3.1 39.1 1.0 N A:ALA100 3.2 35.0 1.0 O A:HOH461 3.3 48.6 1.0 CB A:ALA100 3.6 30.1 1.0 O A:HOH362 3.6 42.5 1.0 N A:LEU99 3.8 36.2 1.0 CB A:SER98 3.9 35.8 1.0 CA A:ALA100 4.0 29.8 1.0 CD1 A:LEU167 4.0 36.1 1.0 CB A:LEU99 4.1 30.6 1.0 OG A:SER98 4.1 35.4 1.0 C A:LEU99 4.2 33.1 1.0 CA A:GLY162 4.2 37.5 1.0 CA A:LEU99 4.2 32.5 1.0 CG1 A:VAL157 4.5 34.7 1.0 N A:GLY162 4.5 39.7 1.0 C A:SER98 4.5 30.9 1.0 CA A:SER98 4.7 40.3 1.0 CD2 A:LEU167 4.8 33.7 1.0 O A:HOH390 4.9 47.7 1.0

J.M.Bradley, J.Fair, A.M.Hemmings, N.E.Le Brun. Key Carboxylate Residues For Iron Transit Through the Prokaryotic Ferritin Syn Ftn. Microbiology (Reading, V. 167 2021ENGL.).
ISSN: ESSN 1465-2080
PubMed: 34825885
DOI: 10.1099/MIC.0.001105