Calcium in PDB 7vve: Complex Structure of A Leaf-Branch Compost Cutinase Variant in Complex with Mono(2-Hydroxyethyl) Terephthalic Acid

All present enzymatic activity of Complex Structure of A Leaf-Branch Compost Cutinase Variant in Complex with Mono(2-Hydroxyethyl) Terephthalic Acid:
3.1.1.101; 3.1.1.74;

The structure of Complex Structure of A Leaf-Branch Compost Cutinase Variant in Complex with Mono(2-Hydroxyethyl) Terephthalic Acid, PDB code: 7vve was solved by D.Niu, W.Zeng, J.W.Huang, C.C.Chen, W.D.Liu, R.T.Guo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.98
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	42.277, 85.09, 147.746, 90, 90, 90
R / Rfree (%)	13.9 / 18.7

The binding sites of Calcium atom in the Complex Structure of A Leaf-Branch Compost Cutinase Variant in Complex with Mono(2-Hydroxyethyl) Terephthalic Acid (pdb code 7vve). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Complex Structure of A Leaf-Branch Compost Cutinase Variant in Complex with Mono(2-Hydroxyethyl) Terephthalic Acid, PDB code: 7vve:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Complex Structure of A Leaf-Branch Compost Cutinase Variant in Complex with Mono(2-Hydroxyethyl) Terephthalic Acid


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Complex Structure of A Leaf-Branch Compost Cutinase Variant in Complex with Mono(2-Hydroxyethyl) Terephthalic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:18.3 occ:1.00 O A:THR195 2.4 7.5 1.0 OD1 A:ASP193 2.5 10.0 1.0 O A:HOH718 2.6 12.2 1.0 OD2 A:ASP193 2.6 9.7 1.0 O A:HOH648 2.6 15.2 1.0 O A:HOH593 2.6 10.8 1.0 OG1 A:THR195 2.7 8.4 1.0 CG A:ASP193 2.9 9.0 1.0 C A:THR195 3.4 9.1 1.0 CB A:THR195 3.6 9.6 1.0 CA A:THR195 3.8 9.5 1.0 N A:THR195 4.1 9.8 1.0 O A:HOH711 4.3 18.6 1.0 CB A:ASP193 4.4 9.5 1.0 O A:HOH557 4.5 41.7 1.0 N A:PHE196 4.6 8.7 1.0 NH1 A:ARG173 4.8 9.6 1.0 O A:HOH732 4.8 40.7 1.0 CG2 A:THR195 4.9 10.1 1.0 OE2 A:GLU176 4.9 14.5 1.0 CA A:PHE196 5.0 8.6 1.0

Calcium binding site 2 out of 2 in the Complex Structure of A Leaf-Branch Compost Cutinase Variant in Complex with Mono(2-Hydroxyethyl) Terephthalic Acid


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Complex Structure of A Leaf-Branch Compost Cutinase Variant in Complex with Mono(2-Hydroxyethyl) Terephthalic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca401 b:18.5 occ:1.00 O B:HOH720 2.3 25.8 1.0 O B:THR195 2.4 14.2 1.0 OG1 B:THR195 2.4 19.4 1.0 OD1 B:ASP193 2.5 17.3 1.0 O B:HOH542 2.6 17.3 1.0 O B:HOH721 2.6 22.1 1.0 O B:HOH702 2.6 18.5 1.0 OD2 B:ASP193 2.7 20.8 1.0 CG B:ASP193 2.9 16.8 1.0 C B:THR195 3.4 16.4 1.0 CB B:THR195 3.5 18.7 1.0 CA B:THR195 3.8 17.1 1.0 N B:THR195 4.0 15.5 1.0 CB B:ASP193 4.4 15.4 1.0 O B:HOH764 4.5 40.5 1.0 NH1 B:ARG173 4.6 15.3 1.0 N B:PHE196 4.6 14.6 1.0 OE2 B:GLU176 4.7 16.4 1.0 CG2 B:THR195 4.8 18.2 1.0 O B:HOH640 4.9 21.7 1.0

W.Zeng, X.Li, Y.Yang, J.Min, J.-W.Huang, W.Liu, D.Niu, X.Yang, X.Han, L.Zhang, L.Dai, C.-C.Chen, R.-T.Guo. Substrate-Binding Mode of A Thermophilic Pet Hydrolase and Engineering the Enzyme to Enhance the Hydrolytic Efficacy. Acs Catalysis V. 12 3033 2022.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.1C05800