Chlorine in PDB 5uxb: Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium, Apoenzyme

The structure of Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium, Apoenzyme, PDB code: 5uxb was solved by P.J.Stogios, T.Skarina, V.Yim, A.Savchenko, W.F.Anderson, Center Forstructural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.75 / 2.79
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	75.933, 79.741, 99.132, 90.00, 90.00, 90.00
R / Rfree (%)	21.9 / 25.2

The binding sites of Chlorine atom in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium, Apoenzyme (pdb code 5uxb). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium, Apoenzyme, PDB code: 5uxb:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium, Apoenzyme


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 Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium, Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:34.7 occ:1.00 OG A:SER86 3.3 39.0 1.0 N A:SER86 3.6 36.2 1.0 CB A:SER86 4.1 38.0 1.0 CA A:THR85 4.2 37.2 1.0 C A:THR85 4.3 35.7 1.0 CB A:THR85 4.4 39.9 1.0 CA A:SER86 4.4 37.5 1.0 CG2 A:THR85 5.0 31.8 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium, Apoenzyme


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 Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium, Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:24.1 occ:1.00 OG B:SER86 3.5 42.9 1.0 N B:SER86 3.7 38.1 1.0 CB B:SER86 4.2 41.6 1.0 CA B:THR85 4.2 34.2 1.0 CB B:THR85 4.2 36.9 1.0 C B:THR85 4.5 35.0 1.0 CA B:SER86 4.6 41.2 1.0 CG2 B:THR85 4.6 34.9 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium, Apoenzyme


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 Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium, Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl302 b:68.8 occ:1.00 CB B:ASP32 3.4 63.0 1.0 N B:ASP32 3.5 73.0 1.0 N B:LEU31 3.8 86.7 1.0 CA B:ASP32 4.0 65.1 1.0 CA B:GLY30 4.0 97.8 1.0 N B:PHE33 4.1 54.3 1.0 CG B:ASP32 4.2 64.1 1.0 C B:GLY30 4.2 94.4 1.0 CD2 B:LEU31 4.2 99.9 1.0 CG B:LEU31 4.2 96.6 1.0 OD2 B:ASP32 4.4 63.9 1.0 C B:LEU31 4.5 81.9 1.0 C B:ASP32 4.6 59.4 1.0 CA B:LEU31 4.6 88.1 1.0 OD1 B:ASP32 4.9 65.4 1.0 O B:PHE33 5.0 50.2 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium, Apoenzyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium, Apoenzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl303 b:40.9 occ:1.00 NZ B:LYS225 2.6 54.1 1.0 CE B:LYS225 3.6 52.4 1.0 O B:HOH458 3.8 42.7 1.0 CG2 B:VAL151 3.8 31.0 1.0 N B:ASP222 3.9 31.0 1.0 CB B:ASP222 4.3 34.8 1.0 CG1 B:VAL151 4.4 25.1 1.0 CA B:GLY221 4.5 34.4 1.0 OE1 B:GLU144 4.6 57.9 1.0 CB B:VAL151 4.7 28.2 1.0 C B:GLY221 4.7 32.6 1.0 CA B:ASP222 4.7 31.0 1.0 CD B:LYS225 4.8 49.5 1.0

A.C.Pawlowski, P.J.Stogios, K.Koteva, T.Skarina, E.Evdokimova, A.Savchenko, G.D.Wright. The Evolution of Substrate Discrimination in Macrolide Antibiotic Resistance Enzymes. Nat Commun V. 9 112 2018.
ISSN: ESSN 2041-1723
PubMed: 29317655
DOI: 10.1038/S41467-017-02680-0