Chlorine in PDB 4utu: Structural and Biochemical Characterization of the N- Acetylmannosamine-6-Phosphate 2-Epimerase From Clostridium Perfringens

All present enzymatic activity of Structural and Biochemical Characterization of the N- Acetylmannosamine-6-Phosphate 2-Epimerase From Clostridium Perfringens:
5.1.3.9;

The structure of Structural and Biochemical Characterization of the N- Acetylmannosamine-6-Phosphate 2-Epimerase From Clostridium Perfringens, PDB code: 4utu was solved by M.C.Pelissier, C.Sebban-Kreuzer, F.Guerlesquin, J.A.Brannigan, G.J.Davies, Y.Bourne, F.Vincent, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.00 / 1.45
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	36.714, 82.147, 75.195, 90.00, 92.48, 90.00
R / Rfree (%)	14.004 / 16.915

The binding sites of Chlorine atom in the Structural and Biochemical Characterization of the N- Acetylmannosamine-6-Phosphate 2-Epimerase From Clostridium Perfringens (pdb code 4utu). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structural and Biochemical Characterization of the N- Acetylmannosamine-6-Phosphate 2-Epimerase From Clostridium Perfringens, PDB code: 4utu:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structural and Biochemical Characterization of the N- Acetylmannosamine-6-Phosphate 2-Epimerase From Clostridium Perfringens


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structural and Biochemical Characterization of the N- Acetylmannosamine-6-Phosphate 2-Epimerase From Clostridium Perfringens within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1221 b:13.1 occ:1.00 O A:HOH2070 3.0 11.8 1.0 O A:HOH2069 3.0 14.3 1.0 N A:GLN210 3.1 8.9 1.0 N A:PRO209 3.4 8.2 1.0 C A:ARG208 3.4 8.2 1.0 CB A:GLN210 3.4 9.1 1.0 CA A:ARG208 3.5 8.0 1.0 CD A:PRO209 3.5 8.6 1.0 CB A:ARG208 3.8 8.4 1.0 CG A:PRO209 3.8 9.6 1.0 CA A:GLN210 3.9 9.1 1.0 CG A:PRO20 3.9 16.3 1.0 CB B:ALA33 3.9 10.8 1.0 C A:PRO209 4.1 9.0 1.0 O A:ARG208 4.1 8.3 1.0 CD A:PRO20 4.2 14.4 1.0 CA A:PRO209 4.2 8.2 1.0 CG A:ARG208 4.2 8.0 1.0 O A:HOH2057 4.4 9.9 1.0 OE1 A:GLU19 4.6 11.8 1.0 N A:GLN211 4.6 9.1 1.0 CB A:PRO209 4.6 9.4 1.0 CG A:LEU21 4.6 11.3 1.0 OE1 A:GLN210 4.7 11.2 1.0 O A:HOH2257 4.7 13.2 1.0 O A:THR207 4.7 8.3 1.0 N A:ARG208 4.8 8.0 1.0 C A:GLN210 4.8 8.4 1.0 CG A:GLN210 4.9 10.4 1.0 CD1 A:LEU21 4.9 9.7 1.0 CA B:ALA33 4.9 9.8 1.0

Chlorine binding site 2 out of 2 in the Structural and Biochemical Characterization of the N- Acetylmannosamine-6-Phosphate 2-Epimerase From Clostridium Perfringens


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structural and Biochemical Characterization of the N- Acetylmannosamine-6-Phosphate 2-Epimerase From Clostridium Perfringens within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1221 b:10.8 occ:1.00 O B:HOH2045 3.0 11.3 1.0 O B:HOH2049 3.1 11.6 1.0 N B:GLN210 3.2 8.4 1.0 CA B:ARG208 3.4 8.6 1.0 N B:PRO209 3.4 7.7 1.0 CB B:GLN210 3.5 9.1 1.0 C B:ARG208 3.5 8.2 1.0 CD B:PRO209 3.5 8.2 1.0 CG B:PRO209 3.8 8.2 1.0 CB B:ARG208 3.8 10.0 1.0 CG B:PRO20 3.8 14.3 1.0 CA B:GLN210 3.9 9.1 1.0 CD B:PRO20 3.9 11.4 1.0 CB A:ALA33 4.0 8.8 1.0 C B:PRO209 4.1 9.0 1.0 O B:ARG208 4.1 8.6 1.0 CG B:ARG208 4.2 9.8 1.0 CA B:PRO209 4.3 8.7 1.0 O B:HOH2032 4.5 10.3 1.0 CB B:PRO209 4.6 9.4 1.0 O B:HOH2203 4.6 12.1 1.0 OE1 B:GLU19 4.7 12.1 1.0 N B:GLN211 4.7 9.5 1.0 OE1 B:GLN210 4.7 12.1 1.0 O B:THR207 4.7 9.3 1.0 CG B:LEU21 4.8 12.5 1.0 N B:ARG208 4.8 7.9 1.0 CG B:GLN210 4.8 10.5 1.0 C B:GLN210 4.9 7.7 1.0 CB B:PRO20 4.9 15.2 1.0 N B:PRO20 4.9 12.2 1.0 O B:HOH2008 5.0 16.1 1.0

M.C.Pelissier, C.Sebban-Kreuzer, F.Guerlesquin, J.A.Brannigan, G.J.Davies, Y.Bourne, F.Vincent. Structural and Functional Characterization of the Clostridium Perfringens N-Acetylmannosamine-6-Phosphate 2-Epimerase Essential For the Sialic Acid Salvage Pathway J.Biol.Chem. 2014.
ISSN: ESSN 1083-351X
PubMed: 25320079
DOI: 10.1074/JBC.M114.604272