Chlorine in PDB 2pfl: Crystal Structure of Pfl From E.Coli

All present enzymatic activity of Crystal Structure of Pfl From E.Coli:
2.3.1.54;

The structure of Crystal Structure of Pfl From E.Coli, PDB code: 2pfl was solved by A.Becker, K.Fritz-Wolf, W.Kabsch, J.Knappe, S.Schultz, A.F.V.Wagner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.90
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	159.020, 159.020, 160.640, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 24.2

The structure of Crystal Structure of Pfl From E.Coli also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of Pfl From E.Coli (pdb code 2pfl). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Pfl From E.Coli, PDB code: 2pfl:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Pfl From E.Coli


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 Pfl From E.Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1001 b:79.4 occ:1.00 O B:HOH2311 3.1 51.6 1.0 O B:HOH2307 3.3 45.6 1.0 CG A:HIS227 4.0 49.5 1.0 CD1 A:LEU197 4.1 56.1 1.0 ND1 A:HIS227 4.1 49.3 1.0 CB A:HIS227 4.3 47.7 1.0 CD2 A:PHE200 4.4 54.7 1.0 CD2 A:HIS227 4.4 50.3 1.0 CG A:PHE200 4.4 53.6 1.0 CE1 A:HIS227 4.5 50.1 1.0 CE2 A:PHE200 4.7 54.2 1.0 NE2 A:HIS227 4.7 51.4 1.0 CA A:ALA224 4.7 47.0 1.0 CD1 A:PHE200 4.8 54.0 1.0 CB A:PHE200 4.8 53.1 1.0 CB A:ALA224 4.9 46.2 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Pfl From E.Coli


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 Pfl From E.Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1002 b:77.8 occ:1.00 O A:HOH2166 3.3 49.4 1.0 CD1 B:LEU197 4.0 47.6 1.0 CD2 B:PHE200 4.1 47.0 1.0 CG B:PHE200 4.2 48.2 1.0 O A:HOH2108 4.2 56.1 1.0 CG B:HIS227 4.3 45.4 1.0 CE2 B:PHE200 4.3 47.6 1.0 ND1 B:HIS227 4.4 45.5 1.0 CD1 B:PHE200 4.6 47.5 1.0 CB B:HIS227 4.6 44.9 1.0 CB B:PHE200 4.6 48.7 1.0 CZ B:PHE200 4.7 48.4 1.0 CD2 B:HIS227 4.7 45.5 1.0 CA B:ALA224 4.7 38.4 1.0 CE1 B:HIS227 4.8 45.6 1.0 CE1 B:PHE200 4.8 47.3 1.0 CB B:ALA224 4.9 37.2 1.0 NE2 B:HIS227 5.0 46.3 1.0

A.Becker, K.Fritz-Wolf, W.Kabsch, J.Knappe, S.Schultz, A.F.Volker Wagner. Structure and Mechanism of the Glycyl Radical Enzyme Pyruvate Formate-Lyase. Nat.Struct.Biol. V. 6 969 1999.
ISSN: ISSN 1072-8368
PubMed: 10504733
DOI: 10.1038/13341