Chlorine in PDB 4jid: Crystal Structure of Baldcb / Vany-Like L,D-Carboxypeptidase Zinc(II)- Free

All present enzymatic activity of Crystal Structure of Baldcb / Vany-Like L,D-Carboxypeptidase Zinc(II)- Free:
3.4.16.4;

The structure of Crystal Structure of Baldcb / Vany-Like L,D-Carboxypeptidase Zinc(II)- Free, PDB code: 4jid was solved by G.Minasov, Z.Wawrzak, O.Onopriyenko, T.Skarina, S.Shatsman, S.N.Peterson, A.Savchenko, W.F.Anderson, Center For Structural Genomics Ofinfectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.71 / 2.30
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	76.576, 112.996, 124.659, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 25.9

The binding sites of Chlorine atom in the Crystal Structure of Baldcb / Vany-Like L,D-Carboxypeptidase Zinc(II)- Free (pdb code 4jid). 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 Baldcb / Vany-Like L,D-Carboxypeptidase Zinc(II)- Free, PDB code: 4jid:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of Baldcb / Vany-Like L,D-Carboxypeptidase Zinc(II)- Free


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 Baldcb / Vany-Like L,D-Carboxypeptidase Zinc(II)- Free within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:43.8 occ:0.75 N A:ILE201 3.3 35.3 1.0 O A:HOH427 3.3 38.7 1.0 CA A:ILE200 3.5 32.8 1.0 O A:HOH423 3.7 47.0 1.0 CB A:ILE200 3.8 33.3 1.0 CD1 A:TYR231 3.9 47.8 1.0 C A:ILE200 3.9 33.4 1.0 CD1 A:ILE201 4.0 40.1 1.0 CB A:TYR231 4.1 49.5 1.0 CG2 A:ILE200 4.2 31.6 1.0 CA A:ILE201 4.3 34.0 1.0 CB A:ILE201 4.4 36.6 1.0 CA A:TYR231 4.4 50.8 1.0 O A:PHE199 4.4 36.9 1.0 CG A:TYR231 4.5 49.8 1.0 O A:ILE201 4.5 38.2 1.0 O A:LYS191 4.6 47.7 1.0 N A:ILE200 4.7 32.5 1.0 CG1 A:ILE201 4.7 38.8 1.0 C A:ILE201 4.8 35.6 1.0 N A:TYR231 4.9 50.2 1.0 CE1 A:TYR231 4.9 48.0 1.0 CB A:ALA194 4.9 31.9 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of Baldcb / Vany-Like L,D-Carboxypeptidase Zinc(II)- Free


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 Baldcb / Vany-Like L,D-Carboxypeptidase Zinc(II)- Free within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:51.7 occ:0.50 O A:LYS205 2.0 60.6 0.5 C A:LYS205 2.9 61.7 0.5 N A:GLY206 3.2 65.7 0.5 O A:HOH507 3.5 55.3 0.5 CA A:LYS205 3.6 59.4 0.5 CA A:LYS205 3.6 58.6 0.5 N A:TYR215 3.7 50.7 1.0 CB A:TYR215 3.8 49.7 1.0 N A:GLY206 3.8 65.8 0.5 C A:LYS205 3.9 61.3 0.5 CA A:GLY206 4.1 69.5 0.5 CA A:GLY206 4.2 69.5 0.5 CB A:LYS205 4.2 60.8 0.5 CA A:TYR215 4.3 47.2 1.0 CG A:LYS205 4.4 59.0 0.5 CB A:LYS205 4.5 62.1 0.5 O A:PRO204 4.6 51.7 1.0 CA A:ALA214 4.6 53.6 1.0 C A:ALA214 4.7 51.3 1.0 N A:LYS205 4.7 55.2 0.5 N A:LYS205 4.8 54.9 0.5 CB A:ALA214 4.8 56.0 1.0 CG A:TYR215 4.9 50.4 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of Baldcb / Vany-Like L,D-Carboxypeptidase Zinc(II)- Free


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 Baldcb / Vany-Like L,D-Carboxypeptidase Zinc(II)- Free within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:51.0 occ:0.50 O A:LYS205 1.8 60.0 0.5 C A:LYS205 2.7 61.3 0.5 N A:LYS205 3.0 54.9 0.5 CB A:LYS205 3.0 62.1 0.5 N A:LYS205 3.1 55.2 0.5 CA A:LYS205 3.1 58.6 0.5 N A:GLY206 3.2 65.8 0.5 CA A:LYS205 3.3 59.4 0.5 CB A:LYS205 3.4 60.8 0.5 C A:PRO204 3.6 52.5 1.0 O A:HOH410 3.6 49.0 1.0 C A:LYS205 3.6 61.7 0.5 CB A:PRO204 3.7 51.0 1.0 N A:GLY206 3.9 65.7 0.5 O A:PRO204 4.1 51.7 1.0 CG A:LYS205 4.1 61.6 0.5 CG A:LYS207 4.2 65.8 1.0 CA A:PRO204 4.2 49.4 1.0 CA A:GLY206 4.3 69.5 0.5 CA A:GLY206 4.4 69.5 0.5 C A:GLY206 4.6 68.8 0.5 N A:LYS207 4.6 65.3 1.0 C A:GLY206 4.7 68.7 0.5 CG A:LYS205 4.7 59.0 0.5 CD A:LYS205 4.8 66.7 0.5 O A:LYS205 4.8 60.6 0.5 CG A:PRO204 4.9 50.1 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of Baldcb / Vany-Like L,D-Carboxypeptidase Zinc(II)- Free


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 Baldcb / Vany-Like L,D-Carboxypeptidase Zinc(II)- Free within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:52.5 occ:0.50 O A:HOH504 2.6 48.6 1.0 O A:HOH512 2.9 57.2 1.0 NZ A:LYS76 3.5 57.2 1.0 CE A:LYS76 3.8 50.0 1.0 CD1 A:LEU80 4.3 32.8 1.0 CZ A:TYR97 4.7 35.0 1.0 CE1 A:TYR97 4.7 33.8 1.0 CE2 A:TYR97 4.8 32.9 1.0 CD1 A:TYR97 5.0 35.3 1.0

C.N.Hoyland, C.Aldridge, R.M.Cleverley, M.C.Duchene, G.Minasov, O.Onopriyenko, K.Sidiq, P.J.Stogios, W.F.Anderson, R.A.Daniel, A.Savchenko, W.Vollmer, R.J.Lewis. Structure of the Ldcb Ld-Carboxypeptidase Reveals the Molecular Basis of Peptidoglycan Recognition. Structure V. 22 949 2014.
ISSN: ISSN 0969-2126
PubMed: 24909784
DOI: 10.1016/J.STR.2014.04.015