Chlorine in PDB 5lui: Structure of Cutinase 1 From Thermobifida Cellulosilytica

The structure of Structure of Cutinase 1 From Thermobifida Cellulosilytica, PDB code: 5lui was solved by A.Hromic, A.Lyskowski, K.Gruber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.42 / 1.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	84.970, 34.890, 78.050, 90.00, 108.56, 90.00
R / Rfree (%)	15.3 / 18.1

The structure of Structure of Cutinase 1 From Thermobifida Cellulosilytica also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Chlorine atom in the Structure of Cutinase 1 From Thermobifida Cellulosilytica (pdb code 5lui). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Structure of Cutinase 1 From Thermobifida Cellulosilytica, PDB code: 5lui:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Structure of Cutinase 1 From Thermobifida Cellulosilytica


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Cutinase 1 From Thermobifida Cellulosilytica within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:8.1 occ:1.00 OG A:SER131 2.8 8.0 1.0 N A:TYR61 3.1 4.0 1.0 O A:HOH502 3.1 14.5 1.0 N A:MET132 3.2 3.1 1.0 CB A:SER131 3.3 6.0 1.0 CG A:MET132 3.4 4.0 1.0 C2 A:PEG301 3.4 21.8 1.0 CB A:TYR61 3.5 4.4 1.0 O2 A:PEG301 3.5 32.7 1.0 CB A:MET132 3.6 2.8 1.0 CA A:TYR61 3.9 2.9 1.0 CA A:GLY60 3.9 6.0 1.0 C A:GLY60 4.0 4.7 1.0 CA A:MET132 4.0 3.6 1.0 C A:SER131 4.1 3.2 1.0 SD A:MET132 4.2 5.1 1.0 CA A:SER131 4.3 4.7 1.0 CE A:MET132 4.5 6.5 1.0 C1 A:PEG301 4.5 17.9 1.0 O A:HOH612 4.5 27.9 1.0 O A:TYR61 4.6 8.1 1.0 C3 A:PEG301 4.7 29.0 1.0 C A:TYR61 4.8 5.8 1.0 CG A:TYR61 4.8 3.9 1.0 NE2 A:HIS209 4.8 6.9 1.0 C4 A:PEG301 4.8 27.6 1.0 CB A:TRP156 4.9 2.8 1.0 O1 A:PEG301 5.0 17.7 1.0 O A:HIS130 5.0 3.1 1.0

Chlorine binding site 2 out of 3 in the Structure of Cutinase 1 From Thermobifida Cellulosilytica


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Cutinase 1 From Thermobifida Cellulosilytica within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl305 b:8.9 occ:1.00 O A:HOH652 3.1 9.9 1.0 CB A:PRO261 3.6 8.9 1.0 N A:PRO261 3.6 6.2 1.0 CA A:PRO261 3.6 6.1 1.0 CB A:CYS260 3.7 6.6 1.0 CD A:PRO261 3.9 7.0 1.0 C A:CYS260 4.0 7.0 1.0 CB A:CYS242 4.0 5.2 1.0 CG A:PRO261 4.0 7.3 1.0 CA A:CYS260 4.4 6.3 1.0 O A:CYS260 4.5 8.1 1.0 SG A:CYS242 4.6 6.5 1.0 O A:HOH574 4.6 11.5 1.0 O A:HOH518 4.7 13.7 1.0 SG A:CYS260 4.9 6.3 1.0

Chlorine binding site 3 out of 3 in the Structure of Cutinase 1 From Thermobifida Cellulosilytica


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of Cutinase 1 From Thermobifida Cellulosilytica within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl306 b:13.4 occ:1.00 N A:THR178 3.2 5.2 1.0 N A:HIS209 3.2 5.7 1.0 OG1 A:THR178 3.3 12.2 1.0 CB A:HIS209 3.5 5.0 1.0 O A:LEU176 3.6 7.6 1.0 CA A:ASP177 3.7 4.8 1.0 CB A:THR208 3.8 7.0 1.0 C A:ASP177 3.9 5.8 1.0 CA A:HIS209 4.0 4.3 1.0 CB A:THR178 4.0 7.8 1.0 CA A:THR178 4.1 6.8 1.0 CA A:THR208 4.1 6.4 1.0 C A:THR208 4.2 6.0 1.0 CG2 A:THR178 4.2 12.9 1.0 OD1 A:ASP177 4.2 5.3 1.0 CD1 A:ILE179 4.4 19.6 1.0 C A:LEU176 4.4 6.6 1.0 N A:ILE179 4.4 4.3 1.0 N A:ASP177 4.5 4.0 1.0 CG1 A:ILE179 4.5 11.0 1.0 OG1 A:THR208 4.6 10.6 1.0 CG2 A:THR208 4.6 11.0 1.0 C A:THR178 4.7 7.7 1.0 CG A:ASP177 4.8 4.6 1.0 CG A:HIS209 4.8 4.8 1.0 CB A:ASP177 4.8 6.4 1.0 CD2 A:PHE210 5.0 14.4 1.0

D.Ribitsch, A.Hromic, S.Zitzenbacher, B.Zartl, C.Gamerith, A.Pellis, A.Jungbauer, A.Yskowski, G.Steinkellner, K.Gruber, R.Tscheliessnig, E.Herrero Acero, G.M.Guebitz. Small Cause, Large Effect: Structural Characterization of Cutinases From Thermobifida Cellulosilytica. Biotechnol. Bioeng. V. 114 2481 2017.
ISSN: ESSN 1097-0290
PubMed: 28671263
DOI: 10.1002/BIT.26372