Calcium in PDB 5mi6: BTGH84 Mutant with Covalent Modification By MA3 in Complex with Thiamet G

All present enzymatic activity of BTGH84 Mutant with Covalent Modification By MA3 in Complex with Thiamet G:
3.2.1.169; 3.2.1.52;

The structure of BTGH84 Mutant with Covalent Modification By MA3 in Complex with Thiamet G, PDB code: 5mi6 was solved by J.F.Darby, G.J.Davies, R.E.Hubbard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.66 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	196.023, 51.662, 112.258, 90.00, 113.34, 90.00
R / Rfree (%)	19.9 / 24

The binding sites of Calcium atom in the BTGH84 Mutant with Covalent Modification By MA3 in Complex with Thiamet G (pdb code 5mi6). 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 BTGH84 Mutant with Covalent Modification By MA3 in Complex with Thiamet G, PDB code: 5mi6:

Calcium binding site 1 out of 1 in the BTGH84 Mutant with Covalent Modification By MA3 in Complex with Thiamet G


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of BTGH84 Mutant with Covalent Modification By MA3 in Complex with Thiamet G within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca806 b:27.4 occ:1.00 O A:HOH1046 2.3 41.0 1.0 O A:HOH1174 2.3 15.9 1.0 O A:GLU32 2.3 27.6 1.0 O A:HOH1148 2.3 32.9 1.0 OE1 A:GLU61 2.4 27.4 1.0 OD1 A:ASP64 2.6 33.4 1.0 OD2 A:ASP64 2.8 31.0 1.0 CG A:ASP64 3.0 31.0 1.0 C A:GLU32 3.5 33.8 1.0 CD A:GLU61 3.6 25.6 1.0 CA A:ALA33 4.2 32.2 1.0 CB A:GLU61 4.2 24.5 1.0 CG A:GLU61 4.3 24.7 1.0 N A:ALA33 4.3 32.2 1.0 OE2 A:GLU61 4.5 26.6 1.0 CB A:ASP64 4.6 29.9 1.0 N A:GLU61 4.6 21.6 1.0 CA A:GLU32 4.6 37.5 1.0 C A:ALA33 4.7 30.2 1.0 CB A:GLU32 4.7 42.4 1.0 N A:ASN34 4.9 30.3 1.0 OE1 A:GLU97 4.9 56.7 1.0 CA A:GLU61 5.0 23.4 1.0

J.F.Darby, M.Atobe, J.D.Firth, P.Bond, G.J.Davies, P.O'brien, R.E.Hubbard. Increase of Enzyme Activity Through Specific Covalent Modification with Fragments. Chem Sci V. 8 7772 2017.
ISSN: ISSN 2041-6520
PubMed: 29163914
DOI: 10.1039/C7SC01966A