Chlorine in PDB 5uxd: Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium in Complex with Azithromycin

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

Resolution Low / High (Å)	45.35 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	55.050, 81.210, 71.340, 90.00, 96.83, 90.00
R / Rfree (%)	19.1 / 23.2

The binding sites of Chlorine atom in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium in Complex with Azithromycin (pdb code 5uxd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 6 binding sites of Chlorine where determined in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium in Complex with Azithromycin, PDB code: 5uxd:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5; 6;

Chlorine binding site 1 out of 6 in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium in Complex with Azithromycin


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 in Complex with Azithromycin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl503 b:29.1 occ:1.00 N A:ASP222 3.3 13.4 1.0 O A:HOH835 3.5 19.6 1.0 CD A:LYS225 3.5 33.4 1.0 O A:HOH745 3.5 25.9 1.0 NE A:ARG146 3.6 32.2 0.4 NH2 A:ARG146 3.6 13.1 0.4 CB A:ASP222 3.6 11.9 1.0 CZ A:ARG146 3.6 20.5 0.4 CG2 A:VAL151 3.8 15.3 1.0 CA A:GLY221 4.0 16.8 1.0 CG1 A:VAL151 4.0 17.0 1.0 CA A:ASP222 4.1 13.3 1.0 C A:GLY221 4.1 12.1 1.0 NZ A:LYS225 4.3 43.7 1.0 O A:HOH1068 4.3 37.6 1.0 NH1 A:ARG146 4.4 30.5 0.4 CG A:LYS225 4.5 27.5 1.0 CE A:LYS225 4.5 37.9 1.0 CB A:VAL151 4.5 13.8 1.0 NH1 A:ARG146 4.6 22.3 0.6 CD A:ARG146 4.6 22.6 0.6 O A:HOH985 4.6 32.7 1.0 CD A:ARG146 4.7 24.2 0.4 CA A:VAL151 5.0 13.4 1.0 CG A:ASP222 5.0 16.6 1.0

Chlorine binding site 2 out of 6 in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium in Complex with Azithromycin


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 in Complex with Azithromycin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl504 b:39.0 occ:1.00 O A:HOH1176 2.9 35.6 1.0 O A:HOH1158 3.2 29.9 0.5 N A:ASP32 3.3 22.9 1.0 N A:PHE33 3.3 20.5 1.0 CA A:GLY30 3.6 29.9 1.0 N A:LEU31 3.6 29.0 1.0 O A:HOH661 3.7 45.3 1.0 C A:GLY30 3.8 31.1 1.0 CB A:ASP32 3.8 24.9 1.0 CA A:ASP32 3.9 24.2 1.0 CD1 A:PHE33 3.9 27.0 1.0 O A:HOH922 3.9 43.6 1.0 C A:ASP32 4.0 27.4 1.0 O A:PHE33 4.1 28.2 1.0 CA A:PHE33 4.2 20.0 1.0 CB A:PHE33 4.2 17.8 1.0 O A:HOH1158 4.3 30.1 0.5 C A:LEU31 4.4 26.3 1.0 O A:HOH722 4.5 38.7 1.0 CA A:LEU31 4.5 32.2 1.0 CG A:PHE33 4.6 28.8 1.0 C A:PHE33 4.6 25.0 1.0 O A:GLY30 4.7 31.1 1.0 CG A:ASP32 4.8 37.9 1.0 CE1 A:PHE33 4.9 20.6 1.0 N A:GLY30 5.0 37.5 1.0 O A:HOH1087 5.0 32.3 1.0

Chlorine binding site 3 out of 6 in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium in Complex with Azithromycin


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 in Complex with Azithromycin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl505 b:77.3 occ:1.00 NH1 A:ARG121 2.4 58.7 1.0 O A:HOH838 3.3 22.3 1.0 NH2 A:ARG208 3.3 57.9 1.0 NE A:ARG208 3.6 54.6 1.0 CZ A:ARG121 3.6 50.2 1.0 CZ A:ARG208 3.9 61.0 1.0 NH2 A:ARG121 4.1 36.0 1.0 O A:HOH1051 4.4 31.8 1.0 NE A:ARG121 4.7 48.2 1.0 CD A:ARG208 4.8 51.6 1.0 CG1 A:VAL118 4.9 19.8 1.0 CG2 A:VAL118 5.0 24.6 1.0

Chlorine binding site 4 out of 6 in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium in Complex with Azithromycin


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 in Complex with Azithromycin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl506 b:51.1 occ:1.00 O A:HOH1066 2.6 43.2 1.0 O A:HOH1044 2.9 33.3 1.0 NH1 A:ARG59 2.9 58.6 1.0 O A:HOH778 3.0 22.9 1.0 O A:HOH761 3.6 22.7 1.0 CZ A:ARG59 4.0 70.4 1.0 CG1 A:VAL62 4.0 22.2 1.0 CB A:VAL62 4.0 22.5 1.0 CG2 A:VAL62 4.2 17.8 1.0 CA A:ARG59 4.3 25.4 1.0 O A:THR216 4.4 23.0 1.0 CB A:ARG59 4.5 31.4 1.0 CG A:ARG59 4.6 47.2 1.0 CD A:ARG59 4.6 54.5 1.0 O A:HOH713 4.6 36.4 1.0 NE A:ARG59 4.7 72.9 1.0 O A:ARG59 4.7 18.5 1.0 NH2 A:ARG59 4.8 58.5 1.0 O A:HOH743 4.8 27.5 1.0 O A:HOH791 4.8 23.9 1.0

Chlorine binding site 5 out of 6 in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium in Complex with Azithromycin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium in Complex with Azithromycin within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl503 b:36.3 occ:1.00 O B:HOH1056 2.7 37.6 1.0 O B:HOH958 3.3 43.7 1.0 N B:ASP32 3.4 24.8 1.0 N B:PHE33 3.6 16.6 1.0 N B:LEU31 3.6 19.7 1.0 O B:HOH919 3.6 34.4 1.0 CA B:GLY30 3.7 24.7 1.0 C B:GLY30 3.9 30.3 1.0 CD1 B:PHE33 4.0 23.2 1.0 CB B:ASP32 4.0 26.0 1.0 O B:HOH824 4.0 44.2 1.0 CA B:ASP32 4.0 22.8 1.0 C B:ASP32 4.2 22.2 1.0 CB B:PHE33 4.3 19.4 1.0 O B:PHE33 4.3 26.8 1.0 O B:HOH795 4.4 37.4 1.0 C B:LEU31 4.4 24.0 1.0 CA B:PHE33 4.4 17.4 1.0 C7A B:ZIT501 4.5 27.6 1.0 CA B:LEU31 4.5 24.4 1.0 O B:HOH663 4.5 30.5 1.0 CG B:PHE33 4.7 29.4 1.0 O B:HOH1037 4.7 42.6 1.0 O B:HOH840 4.8 47.6 1.0 OD2 B:ASP214 4.8 49.3 1.0 O B:GLY30 4.9 24.0 1.0 C B:PHE33 4.9 19.9 1.0 CE1 B:PHE33 4.9 31.4 1.0

Chlorine binding site 6 out of 6 in the Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium in Complex with Azithromycin


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 6 of Crystal Structure of Macrolide 2'-Phosphotransferase Mphh From Brachybacterium Faecium in Complex with Azithromycin within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl504 b:53.4 occ:1.00 O B:HOH1061 3.5 51.4 1.0 N B:SER236 3.8 19.1 1.0 O B:HOH951 3.9 50.2 1.0 OG B:SER236 4.1 39.6 1.0 CA B:PRO235 4.3 22.7 1.0 CB B:SER236 4.3 29.1 1.0 O B:HOH823 4.3 29.3 1.0 C B:PRO235 4.6 26.0 1.0 CA B:SER236 4.7 20.0 1.0 CB B:PRO235 4.7 21.2 1.0 O B:HOH671 4.9 31.4 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