Chlorine in PDB 4azk: Structural Basis of L-Phosphoserine Binding to Bacillus Alcalophilus Phosphoserine Aminotransferase

All present enzymatic activity of Structural Basis of L-Phosphoserine Binding to Bacillus Alcalophilus Phosphoserine Aminotransferase:
2.6.1.52;

The structure of Structural Basis of L-Phosphoserine Binding to Bacillus Alcalophilus Phosphoserine Aminotransferase, PDB code: 4azk was solved by P.Battula, A.P.Dubnovitsky, A.C.Papageorgiou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.32 / 1.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	105.598, 136.599, 152.004, 90.00, 90.00, 90.00
R / Rfree (%)	15.4 / 17.1

The binding sites of Chlorine atom in the Structural Basis of L-Phosphoserine Binding to Bacillus Alcalophilus Phosphoserine Aminotransferase (pdb code 4azk). 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 Basis of L-Phosphoserine Binding to Bacillus Alcalophilus Phosphoserine Aminotransferase, PDB code: 4azk:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structural Basis of L-Phosphoserine Binding to Bacillus Alcalophilus Phosphoserine Aminotransferase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structural Basis of L-Phosphoserine Binding to Bacillus Alcalophilus Phosphoserine Aminotransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1362 b:10.3 occ:1.00 O B:HOH2228 3.1 10.0 1.0 N B:SER101 3.3 9.9 1.0 N B:ILE153 3.4 9.6 1.0 C B:ASN151 3.5 8.9 1.0 CB B:ILE153 3.6 8.8 1.0 N B:THR152 3.6 8.3 1.0 CB B:ASN151 3.6 8.6 1.0 CA B:ASN151 3.6 7.7 1.0 N B:TRP102 3.7 10.2 1.0 CD1 B:TRP102 3.7 11.1 1.0 CD2 B:TYR154 3.8 8.7 1.0 CA B:GLY100 3.8 9.1 1.0 C B:GLY100 3.9 11.2 1.0 N B:TYR154 3.9 9.3 1.0 CA B:ILE153 3.9 10.0 1.0 O B:ASN151 3.9 8.7 1.0 CA B:SER101 4.1 9.6 1.0 CB B:SER101 4.1 13.6 1.0 CG B:TRP102 4.3 9.8 1.0 CG1 B:ILE153 4.3 9.4 1.0 CB B:TRP102 4.4 9.4 1.0 C B:THR152 4.4 10.3 1.0 C B:SER101 4.4 12.5 1.0 CD1 B:ILE153 4.4 11.8 1.0 C B:ILE153 4.4 10.5 1.0 CA B:THR152 4.5 8.9 1.0 CE2 B:TYR154 4.5 9.9 1.0 CG2 B:ILE153 4.5 11.6 1.0 NE1 B:TRP102 4.6 10.6 1.0 OD1 B:ASN151 4.6 9.3 1.0 CG B:ASN151 4.6 8.3 1.0 CA B:TRP102 4.6 9.0 1.0 CB B:TYR154 4.7 11.1 1.0 CG B:TYR154 4.7 10.4 1.0 N B:GLY100 4.8 8.1 1.0 O B:GLY100 5.0 9.4 1.0 CA B:TYR154 5.0 8.5 1.0 O B:THR99 5.0 9.4 1.0

Chlorine binding site 2 out of 2 in the Structural Basis of L-Phosphoserine Binding to Bacillus Alcalophilus Phosphoserine Aminotransferase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structural Basis of L-Phosphoserine Binding to Bacillus Alcalophilus Phosphoserine Aminotransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1362 b:11.6 occ:1.00 O A:HOH2235 3.1 11.8 1.0 N A:SER101 3.3 11.8 1.0 N A:ILE153 3.3 12.9 1.0 C A:ASN151 3.5 11.9 1.0 CB A:ILE153 3.6 10.1 1.0 N A:THR152 3.6 10.6 1.0 N A:TRP102 3.6 11.4 1.0 CD1 A:TRP102 3.7 9.8 1.0 CA A:ASN151 3.7 10.2 1.0 CB A:ASN151 3.7 10.7 1.0 CD2 A:TYR154 3.8 10.5 1.0 CA A:GLY100 3.8 11.2 1.0 C A:GLY100 3.9 11.9 1.0 CA A:ILE153 3.9 11.0 1.0 N A:TYR154 3.9 10.2 1.0 O A:ASN151 3.9 12.6 1.0 CA A:SER101 4.1 12.6 1.0 CB A:SER101 4.2 16.0 1.0 CG1 A:ILE153 4.3 13.6 1.0 CG A:TRP102 4.3 10.5 1.0 CB A:TRP102 4.3 11.1 1.0 C A:THR152 4.3 12.3 1.0 C A:SER101 4.4 12.7 1.0 C A:ILE153 4.4 12.7 1.0 CA A:THR152 4.4 11.3 1.0 CE2 A:TYR154 4.5 13.6 1.0 CD1 A:ILE153 4.5 15.9 1.0 NE1 A:TRP102 4.6 10.7 1.0 CA A:TRP102 4.6 10.7 1.0 CG2 A:ILE153 4.6 12.3 1.0 OD1 A:ASN151 4.6 10.5 1.0 CG A:ASN151 4.7 11.7 1.0 CG A:TYR154 4.7 14.2 1.0 CB A:TYR154 4.7 13.0 1.0 N A:GLY100 4.8 11.2 1.0 O A:GLY100 4.9 13.1 1.0 CA A:TYR154 4.9 11.3 1.0 CB A:THR152 5.0 12.2 1.0 O A:THR99 5.0 13.0 1.0

P.Battula, A.P.Dubnovitsky, A.C.Papageorgiou. Structural Basis of L-Phosphoserine Binding to Bacillus Alcalophilus Phosphoserine Aminotransferase Acta Crystallogr.,Sect.D V. 69 804 2013.
ISSN: ISSN 0907-4449
PubMed: 23633589
DOI: 10.1107/S0907444913002096