Magnesium 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:

Chlorine

(Cl)

3 atoms

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

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Cutinase 1 From Thermobifida Cellulosilytica within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:9.1 occ:1.00 OE1 A:GLU254 2.0 10.6 0.4 OD2 A:ASP175 2.1 7.1 1.0 O A:HOH485 2.1 13.2 1.0 O A:HOH587 2.1 11.9 1.0 OD1 A:ASP205 2.1 9.6 1.0 OE1 A:GLU254 2.1 10.5 0.6 O A:HOH569 2.1 11.1 1.0 CD A:GLU254 3.1 11.7 0.4 CG A:ASP175 3.2 6.9 1.0 CD A:GLU254 3.2 8.9 0.6 CG A:ASP205 3.3 12.0 1.0 OE2 A:GLU254 3.6 17.2 0.4 CB A:ASP175 3.7 6.9 1.0 N A:GLY206 3.9 7.6 1.0 O A:HOH451 3.9 23.0 1.0 OE2 A:GLU254 4.0 11.7 0.6 OD2 A:ASP205 4.1 16.3 1.0 CA A:ASP205 4.1 6.8 1.0 O A:HOH615 4.2 19.7 1.0 O A:HOH411 4.2 17.3 1.0 CB A:ASP205 4.2 8.5 1.0 OD1 A:ASP175 4.2 6.7 1.0 CG A:GLU254 4.3 9.5 0.6 CG A:GLU254 4.3 10.1 0.4 CB A:GLU254 4.4 10.8 0.6 C A:ASP205 4.5 8.3 1.0 CB A:GLU254 4.6 10.5 0.4 CA A:GLY206 4.9 9.1 1.0

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Cutinase 1 From Thermobifida Cellulosilytica within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:17.6 occ:1.00 O A:HOH402 1.9 24.2 1.0 O A:HOH657 2.0 19.5 1.0 O A:HOH404 2.1 17.4 1.0 O A:HOH425 2.1 17.2 1.0 OD1 A:ASN29 2.4 25.4 1.0 CG A:ASN29 3.2 28.3 1.0 ND2 A:ASN29 3.3 25.4 1.0 O A:VAL30 3.8 19.6 1.0 O A:HOH410 4.2 20.3 1.0 O A:HOH594 4.2 24.0 1.0 O A:GLY41 4.3 13.9 1.0 OE2 A:GLU65 4.4 16.7 1.0 C A:VAL30 4.4 22.9 1.0 CB A:ASN29 4.6 21.6 1.0 O A:HOH401 4.6 26.2 1.0 N A:VAL30 4.7 14.6 1.0 CA A:SER31 4.8 28.1 1.0 N A:SER31 4.8 22.7 1.0 N A:GLY41 5.0 11.3 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