Magnesium in PDB 7qjt: Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711)

The structure of Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711), PDB code: 7qjt was solved by M.Zahn, T.J.Shakespeare, G.T.Beckham, J.E.Mcgeehan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	77.29 / 1.78
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	109.297, 109.297, 44.184, 90, 90, 90
R / Rfree (%)	18.2 / 24.2

The binding sites of Magnesium atom in the Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711) (pdb code 7qjt). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711), PDB code: 7qjt:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:2.1 occ:1.00 HE2 A:HIS267 1.0 34.9 0.0 HE2 A:HIS265 1.1 23.4 0.0 H2 A:ALA1 1.2 18.9 1.0 NE2 A:HIS267 1.8 32.7 1.0 NE2 A:HIS265 1.9 22.6 1.0 O A:ALA1 1.9 18.0 1.0 N A:ALA1 2.1 19.8 1.0 H3 A:ALA1 2.5 19.4 1.0 H1 A:ALA1 2.6 19.4 1.0 CE1 A:HIS267 2.8 31.4 1.0 CD2 A:HIS267 2.8 32.9 1.0 C A:ALA1 2.9 18.6 1.0 CE1 A:HIS265 2.9 22.4 1.0 CD2 A:HIS265 2.9 23.1 1.0 HD2 A:HIS267 3.1 32.6 1.0 HE1 A:HIS267 3.1 31.8 1.0 CA A:ALA1 3.1 18.7 1.0 HE1 A:HIS265 3.1 22.2 1.0 HD2 A:HIS265 3.1 23.4 1.0 HA A:ALA1 3.7 18.8 1.0 HD3 A:PRO3 3.8 20.4 1.0 ND1 A:HIS267 3.9 32.1 1.0 ND1 A:HIS265 3.9 22.5 1.0 CG A:HIS267 4.0 32.6 1.0 HB3 A:ALA1 4.0 18.6 1.0 CG A:HIS265 4.0 23.4 1.0 N A:ASN2 4.1 18.3 1.0 CB A:ALA1 4.1 18.5 1.0 O A:HOH515 4.4 34.4 1.0 HA A:ASN2 4.6 19.1 1.0 HB2 A:ALA1 4.6 18.7 1.0 O A:HOH578 4.7 24.1 1.0 CD A:PRO3 4.7 20.2 1.0 HD1 A:HIS267 4.7 33.9 0.0 HB3 A:PRO3 4.8 20.6 1.0 HD1 A:HIS265 4.8 23.4 0.0 H A:ASN2 4.8 18.6 1.0 HB1 A:ALA1 4.8 18.4 1.0 CA A:ASN2 4.8 19.3 1.0 N A:PRO3 4.9 20.0 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg304 b:23.1 occ:1.00 O A:HOH475 1.9 21.1 1.0 OE1 A:GLU201 2.0 19.5 1.0 O A:HOH414 2.0 20.2 1.0 OE2 A:GLU185 2.1 16.7 1.0 OE2 A:GLU253 2.1 17.4 1.0 O A:HOH444 2.1 23.4 1.0 CD A:GLU201 3.0 19.9 1.0 CD A:GLU185 3.2 17.6 1.0 CD A:GLU253 3.2 17.5 1.0 HG2 A:GLU253 3.2 17.5 1.0 OE2 A:GLU201 3.3 21.9 1.0 HE2 A:TYR199 3.6 16.8 1.0 HH21 A:ARG255 3.6 20.1 1.0 OE1 A:GLU185 3.7 17.8 1.0 CG A:GLU253 3.7 17.3 1.0 HG22 A:VAL180 3.8 14.5 1.0 O A:HOH540 3.9 36.3 1.0 HG23 A:VAL180 4.0 14.6 1.0 OH A:TYR199 4.1 17.4 1.0 HG3 A:GLU253 4.1 17.3 1.0 OE1 A:GLU253 4.3 17.8 1.0 HB2 A:GLU201 4.3 18.4 1.0 NH2 A:ARG255 4.3 20.4 1.0 O A:HOH615 4.3 45.0 1.0 CG A:GLU201 4.3 18.9 1.0 CG2 A:VAL180 4.4 14.5 1.0 CE2 A:TYR199 4.4 16.6 1.0 HG2 A:GLU252 4.4 27.1 1.0 HH22 A:ARG255 4.5 20.1 1.0 CG A:GLU185 4.5 17.4 1.0 HG2 A:GLU185 4.5 17.3 1.0 HG3 A:GLU252 4.6 27.1 1.0 HB3 A:GLU201 4.6 18.5 1.0 CB A:GLU201 4.7 18.4 1.0 HG3 A:GLU185 4.7 17.3 1.0 HH A:TYR199 4.7 17.6 0.0 CZ A:TYR199 4.8 16.8 1.0 HG3 A:GLU201 4.8 18.9 1.0 HG2 A:GLU201 5.0 19.1 1.0 HB3 A:GLU253 5.0 18.3 1.0 HG21 A:VAL180 5.0 14.6 1.0 CG A:GLU252 5.0 27.3 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of A Cutinase Enzyme From Thermobifida Cellulosilytica TB100 (711) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg305 b:38.3 occ:1.00 OD1 A:ASN203 1.9 35.1 1.0 OE1 A:GLU252 2.0 32.8 1.0 O A:HOH497 2.4 41.4 1.0 O A:HOH526 2.5 37.0 1.0 OE1 A:GLU173 2.6 29.3 1.0 OE2 A:GLU173 3.0 33.4 1.0 CD A:GLU252 3.0 29.2 1.0 CG A:ASN203 3.0 34.0 1.0 CD A:GLU173 3.1 28.3 1.0 HD21 A:ASN203 3.3 35.4 1.0 HB2 A:GLU252 3.5 24.7 1.0 OE2 A:GLU252 3.6 31.6 1.0 ND2 A:ASN203 3.6 35.8 1.0 HA A:ASN203 3.8 25.6 1.0 CG A:GLU252 4.0 27.3 1.0 HA A:GLU252 4.1 22.1 1.0 H A:GLY204 4.1 24.9 1.0 CB A:GLU252 4.2 25.1 1.0 HG2 A:GLU252 4.3 27.1 1.0 CB A:ASN203 4.3 29.0 1.0 HD22 A:ASN203 4.5 35.2 1.0 CA A:ASN203 4.5 25.6 1.0 CG A:GLU173 4.6 25.3 1.0 CA A:GLU252 4.7 21.6 1.0 N A:GLY204 4.7 25.3 1.0 HB3 A:ASN203 4.8 29.3 1.0 HG3 A:GLU252 4.9 27.1 1.0 HG3 A:GLU173 4.9 25.5 1.0 HB2 A:GLU173 4.9 23.4 1.0 HB2 A:ASN203 4.9 29.1 1.0

E.Erickson, J.E.Gado, L.Avilan, F.Bratti, R.K.Brizendine, P.A.Cox, R.Gill, R.Graham, D.J.Kim, G.Konig, W.E.Michener, S.Poudel, K.J.Ramirez, T.J.Shakespeare, M.Zahn, E.S.Boyd, C.M.Payne, J.L.Dubois, A.R.Pickford, G.T.Beckham, J.E.Mcgeehan. Sourcing Thermotolerant Poly(Ethylene Terephthalate) Hydrolase Scaffolds From Natural Diversity Nat Commun V. 13 7850 2022.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-022-35237-X