Chlorine in PDB 4rz6: Transaldolase B E96Q F178Y From E.Coli

All present enzymatic activity of Transaldolase B E96Q F178Y From E.Coli:
2.2.1.2;

The structure of Transaldolase B E96Q F178Y From E.Coli, PDB code: 4rz6 was solved by L.Stellmacher, T.Sandalova, S.Leptihn, G.Schneider, G.A.Sprenger, A.K.Samland, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.07 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	67.844, 89.513, 130.512, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 24.9

The binding sites of Chlorine atom in the Transaldolase B E96Q F178Y From E.Coli (pdb code 4rz6). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Transaldolase B E96Q F178Y From E.Coli, PDB code: 4rz6:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Transaldolase B E96Q F178Y From E.Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Transaldolase B E96Q F178Y From E.Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:39.9 occ:1.00 O B:HOH518 2.9 21.1 1.0 OH B:TYR103 2.9 18.1 1.0 C12 A:P6G403 3.0 34.5 1.0 O13 A:P6G403 3.1 41.8 1.0 OD1 A:ASN286 3.4 19.8 1.0 CD2 B:LEU295 3.6 19.3 1.0 CE1 B:TYR103 3.6 20.6 1.0 C14 A:P6G403 3.7 36.4 1.0 CZ B:TYR103 3.7 19.1 1.0 CG B:LEU295 3.8 18.5 1.0 CG A:ASN286 3.8 18.9 1.0 N B:ALA296 4.0 16.3 1.0 CB B:ALA296 4.1 18.4 1.0 CA B:ALA296 4.1 18.1 1.0 ND2 A:ASN286 4.1 20.8 1.0 O B:HOH546 4.2 19.6 1.0 CB B:LEU295 4.4 18.3 1.0 C11 A:P6G403 4.5 37.2 1.0 O A:HOH578 4.5 20.1 1.0 C B:LEU295 4.5 17.3 1.0 CG2 B:THR136 4.7 16.5 1.0 CB A:ASN286 4.7 18.8 1.0 C9 A:P6G403 4.9 34.2 1.0 CD1 B:ILE299 4.9 17.2 1.0 O10 A:P6G403 4.9 43.6 1.0 CD1 B:TYR103 4.9 20.7 1.0 NE2 B:HIS285 5.0 18.7 1.0

Chlorine binding site 2 out of 4 in the Transaldolase B E96Q F178Y From E.Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Transaldolase B E96Q F178Y From E.Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl403 b:41.5 occ:1.00 O A:HOH504 2.8 21.8 1.0 O B:ALA296 2.8 16.3 1.0 OH B:TYR103 3.1 18.1 1.0 O A:ASN286 3.3 21.2 1.0 CB A:ASN286 3.4 18.8 1.0 CG2 B:ILE299 3.5 17.3 1.0 CA B:ALA296 3.5 18.1 1.0 C B:ALA296 3.5 17.0 1.0 CB B:ILE299 3.5 17.1 1.0 CG B:ARG300 3.7 20.6 1.0 CB B:ALA296 3.8 18.4 1.0 CE2 B:TYR103 3.8 19.9 1.0 C A:ASN286 3.9 18.3 1.0 CZ B:TYR103 3.9 19.1 1.0 N B:ARG300 4.0 19.5 1.0 CA A:ASN286 4.3 17.4 1.0 C B:ILE299 4.5 20.3 1.0 CA B:ILE299 4.5 18.1 1.0 CD1 B:ILE299 4.5 17.2 1.0 CG A:ASN286 4.5 18.9 1.0 OE1 A:GLN287 4.5 47.5 1.0 CG1 B:ILE299 4.6 18.4 1.0 CA B:ARG300 4.6 20.9 1.0 NH1 B:ARG300 4.7 18.8 1.0 CB B:ARG300 4.7 21.2 1.0 N A:GLN287 4.7 20.6 1.0 CD B:ARG300 4.7 19.1 1.0 N B:GLU297 4.8 17.5 1.0 N B:ALA296 4.8 16.3 1.0 O B:LEU295 4.8 16.9 1.0 CZ3 A:TRP283 4.9 17.4 1.0 OD1 A:ASN286 4.9 19.8 1.0 N B:ILE299 4.9 18.2 1.0

Chlorine binding site 3 out of 4 in the Transaldolase B E96Q F178Y From E.Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Transaldolase B E96Q F178Y From E.Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl404 b:41.9 occ:1.00 O B:HOH501 2.6 19.9 1.0 O B:HOH517 2.9 22.4 1.0 OG B:SER108 3.0 19.6 1.0 CG2 B:VAL97 3.3 26.4 1.0 CA B:SER102 3.6 20.4 1.0 CB B:SER108 3.7 18.9 1.0 O B:LEU101 3.8 18.0 1.0 C B:LEU101 3.9 20.4 1.0 N B:SER102 3.9 20.4 1.0 CB B:LEU133 3.9 29.1 1.0 CD2 B:LEU133 4.0 30.9 1.0 OG B:SER102 4.2 19.1 1.0 CG B:LEU133 4.3 31.7 1.0 CA B:LEU133 4.3 23.7 1.0 N B:ALA134 4.4 17.3 1.0 CB B:SER102 4.4 19.6 1.0 C B:SER102 4.4 18.4 1.0 CB B:LEU101 4.5 19.9 1.0 O B:SER102 4.5 17.6 1.0 O B:ASP98 4.6 22.6 1.0 CB B:VAL97 4.7 25.8 1.0 CA B:LEU101 4.8 20.2 1.0 CA B:SER108 4.8 19.1 1.0 C B:LEU133 4.9 20.2 1.0 O B:HOH560 5.0 20.5 1.0

Chlorine binding site 4 out of 4 in the Transaldolase B E96Q F178Y From E.Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Transaldolase B E96Q F178Y From E.Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl405 b:45.0 occ:1.00 O B:HOH502 2.5 29.5 1.0 O B:HOH561 2.9 27.1 1.0 O B:HOH633 2.9 35.8 1.0 CA B:LYS111 3.5 24.3 1.0 N B:LYS111 3.6 21.0 1.0 CD B:LYS111 3.6 31.1 1.0 C B:ALA110 3.7 21.9 1.0 O B:ALA110 3.8 23.1 1.0 CB B:ALA110 4.0 21.8 1.0 CB B:LYS111 4.0 25.4 1.0 CB B:ARG114 4.1 23.7 1.0 O B:HOH531 4.4 27.6 1.0 NZ B:LYS111 4.4 38.0 1.0 CG B:LYS111 4.5 27.5 1.0 O B:HOH687 4.5 52.2 1.0 CA B:ALA110 4.5 22.9 1.0 CE B:LYS111 4.6 36.9 1.0 CG B:ARG114 4.6 27.6 1.0 O B:HOH600 4.7 35.7 1.0 O B:ALA107 4.7 21.2 1.0 C B:LYS111 4.8 23.9 1.0 O B:HOH666 4.8 44.6 1.0

L.Stellmacher, T.Sandalova, S.Leptihn, G.Schneider, G.A.Sprenger, A.K.Samland. Acid Base Catalyst Discriminates Between A Fructose 6-Phosphate Aldolase and A Transaldolase Chemcatchem 2015.
ISSN: ESSN 1867-3899
DOI: 10.1002/CCTC.201500478