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Calcium in PDB 8jmp: Structure of A Leaf-Branch Compost Cutinase, Iccg in Complex with 1,4- Butanediol Terephthalate

Enzymatic activity of Structure of A Leaf-Branch Compost Cutinase, Iccg in Complex with 1,4- Butanediol Terephthalate

All present enzymatic activity of Structure of A Leaf-Branch Compost Cutinase, Iccg in Complex with 1,4- Butanediol Terephthalate:
3.1.1.101; 3.1.1.74;

Protein crystallography data

The structure of Structure of A Leaf-Branch Compost Cutinase, Iccg in Complex with 1,4- Butanediol Terephthalate, PDB code: 8jmp was solved by Y.Yang, T.Xue, Y.Zheng, S.Cheng, R.-T.Guo, C.-C.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.62 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.19, 84.928, 147.979, 90, 90, 90
R / Rfree (%) 15.4 / 19.6

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of A Leaf-Branch Compost Cutinase, Iccg in Complex with 1,4- Butanediol Terephthalate (pdb code 8jmp). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure of A Leaf-Branch Compost Cutinase, Iccg in Complex with 1,4- Butanediol Terephthalate, PDB code: 8jmp:

Calcium binding site 1 out of 1 in 8jmp

Go back to Calcium Binding Sites List in 8jmp
Calcium binding site 1 out of 1 in the Structure of A Leaf-Branch Compost Cutinase, Iccg in Complex with 1,4- Butanediol Terephthalate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of A Leaf-Branch Compost Cutinase, Iccg in Complex with 1,4- Butanediol Terephthalate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca401

b:11.9
occ:1.00
 O A:THR195 2.3 10.0 1.0
O A:HOH681 2.4 15.8 1.0
OD2 A:ASP193 2.5 12.2 1.0
OD1 A:ASP193 2.5 12.4 1.0
O A:HOH634 2.5 12.3 1.0
OG1 A:THR195 2.5 11.4 1.0
CG A:ASP193 2.8 12.5 1.0
C A:THR195 3.4 12.4 1.0
CB A:THR195 3.6 9.1 1.0
CA A:THR195 3.9 10.3 1.0
N A:THR195 4.1 9.9 1.0
O A:HOH720 4.2 25.8 1.0
CB A:ASP193 4.3 10.9 1.0
N A:PHE196 4.6 13.4 1.0
O A:HOH755 4.6 29.1 1.0
NH1 A:ARG173 4.7 13.6 1.0
O A:HOH671 4.7 31.8 1.0
CG2 A:THR195 4.9 10.3 1.0
OE2 A:GLU176 4.9 15.7 1.0
CA A:PHE196 5.0 10.8 1.0

Reference:

Y.Yang, S.Cheng, Y.Zheng, T.Xue, J.W.Huang, L.Zhang, Y.Yang, R.T.Guo, C.C.Chen. Remodeling the Polymer-Binding Cavity to Improve the Efficacy of Pbat-Degrading Enzyme. J Hazard Mater V. 464 32965 2023.
ISSN: ESSN 1873-3336
PubMed: 37979420
DOI: 10.1016/J.JHAZMAT.2023.132965
Page generated: Thu Dec 28 01:42:53 2023

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