Chlorine in PDB 5yd2: Crystal Structure of Delta 4 Mutant of Ehpsat (Phosphoserine Aminotransferase of Entamoeba Histolytica)

The structure of Crystal Structure of Delta 4 Mutant of Ehpsat (Phosphoserine Aminotransferase of Entamoeba Histolytica), PDB code: 5yd2 was solved by R.K.Singh, S.Gourinath, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.35
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	132.238, 67.904, 95.030, 90.00, 110.93, 90.00
R / Rfree (%)	22.9 / 28.7

The binding sites of Chlorine atom in the Crystal Structure of Delta 4 Mutant of Ehpsat (Phosphoserine Aminotransferase of Entamoeba Histolytica) (pdb code 5yd2). 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 Delta 4 Mutant of Ehpsat (Phosphoserine Aminotransferase of Entamoeba Histolytica), PDB code: 5yd2:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Delta 4 Mutant of Ehpsat (Phosphoserine Aminotransferase of Entamoeba Histolytica)


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 Delta 4 Mutant of Ehpsat (Phosphoserine Aminotransferase of Entamoeba Histolytica) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:49.0 occ:1.00 O A:HOH505 2.8 46.9 1.0 N A:VAL96 3.2 48.1 1.0 N A:ILE145 3.5 46.5 1.0 C A:ASN143 3.6 49.5 1.0 N A:THR144 3.6 47.0 1.0 CB A:ASN143 3.7 49.9 1.0 CA A:GLY95 3.7 48.4 1.0 CD2 A:TYR146 3.7 48.6 1.0 CA A:ASN143 3.8 47.2 1.0 N A:TRP97 3.8 47.3 1.0 CB A:ILE145 3.8 51.3 1.0 CD1 A:TRP97 3.8 47.5 1.0 C A:GLY95 3.8 49.2 1.0 CA A:VAL96 4.1 49.0 1.0 O A:ASN143 4.1 60.3 1.0 CA A:ILE145 4.1 49.9 1.0 CB A:VAL96 4.2 50.1 1.0 CE2 A:TYR146 4.2 50.7 1.0 N A:TYR146 4.3 48.8 1.0 CG1 A:ILE145 4.4 54.3 1.0 OD1 A:ASN143 4.4 46.9 1.0 C A:VAL96 4.4 48.6 1.0 C A:THR144 4.5 46.1 1.0 CA A:THR144 4.5 46.5 1.0 CG A:TRP97 4.5 45.5 1.0 CG A:ASN143 4.6 49.2 1.0 NE1 A:TRP97 4.6 46.0 1.0 O A:THR94 4.6 47.7 1.0 CD1 A:ILE145 4.7 52.9 1.0 CB A:TRP97 4.7 47.1 1.0 C A:ILE145 4.7 49.5 1.0 CG A:TYR146 4.7 52.5 1.0 CA A:TRP97 4.8 46.4 1.0 N A:GLY95 4.8 50.3 1.0 CG2 A:VAL96 4.9 50.2 1.0 CG2 A:ILE145 4.9 53.1 1.0 O A:GLY95 4.9 52.2 1.0 CB A:TYR146 5.0 50.2 1.0 CB A:THR144 5.0 45.4 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Delta 4 Mutant of Ehpsat (Phosphoserine Aminotransferase of Entamoeba Histolytica)


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 Delta 4 Mutant of Ehpsat (Phosphoserine Aminotransferase of Entamoeba Histolytica) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl401 b:53.2 occ:1.00 N B:VAL96 3.2 47.4 1.0 N B:ILE145 3.5 52.9 1.0 CD1 B:TRP97 3.6 49.6 1.0 N B:TRP97 3.6 51.1 1.0 N B:THR144 3.7 53.0 1.0 C B:ASN143 3.7 56.2 1.0 CB B:ILE145 3.8 51.4 1.0 CA B:GLY95 3.8 48.7 1.0 C B:GLY95 3.9 47.6 1.0 CB B:ASN143 3.9 56.1 1.0 CA B:ASN143 3.9 53.5 1.0 CD2 B:TYR146 3.9 55.0 1.0 CA B:VAL96 4.0 49.0 1.0 CB B:VAL96 4.0 48.4 1.0 CA B:ILE145 4.2 52.1 1.0 O B:ASN143 4.3 64.5 1.0 CG B:TRP97 4.3 49.5 1.0 NE1 B:TRP97 4.3 49.5 1.0 C B:VAL96 4.3 50.6 1.0 CG1 B:ILE145 4.3 48.9 1.0 CE2 B:TYR146 4.3 54.4 1.0 N B:TYR146 4.4 54.1 1.0 C B:THR144 4.5 50.6 1.0 CB B:TRP97 4.5 49.3 1.0 CD1 B:ILE145 4.5 48.3 1.0 CA B:THR144 4.5 50.9 1.0 OD1 B:ASN143 4.6 52.4 1.0 CA B:TRP97 4.7 51.9 1.0 CG B:ASN143 4.8 56.6 1.0 C B:ILE145 4.8 53.3 1.0 O B:THR94 4.8 54.4 1.0 CG2 B:VAL96 4.8 46.4 1.0 CB B:THR144 4.9 49.4 1.0 CG2 B:ILE145 4.9 49.1 1.0 CG B:TYR146 4.9 53.0 1.0 O B:GLY95 4.9 50.1 1.0 N B:GLY95 5.0 48.4 1.0

R.K.Singh, P.Tomar, S.Dharavath, S.Kumar, S.Gourinath. N-Terminal Residues Are Crucial For Quaternary Structure and Active Site Conformation For the Phosphoserine Aminotransferase From Enteric Human Parasite E. Histolytica. Int.J.Biol.Macromol. V. 132 1012 2019.
ISSN: ISSN 0141-8130
PubMed: 30959130
DOI: 10.1016/J.IJBIOMAC.2019.04.027