Magnesium in PDB 6no2: Adp Bound to K114BD Mutant Atp-Grasp Fold of Blastocystis Hominis Succinyl-Coa Synthetase

All present enzymatic activity of Adp Bound to K114BD Mutant Atp-Grasp Fold of Blastocystis Hominis Succinyl-Coa Synthetase:
6.2.1.5;

The structure of Adp Bound to K114BD Mutant Atp-Grasp Fold of Blastocystis Hominis Succinyl-Coa Synthetase, PDB code: 6no2 was solved by J.Huang, M.E.Fraser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.54 / 2.16
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	114.021, 77.748, 77.112, 90.00, 125.17, 90.00
R / Rfree (%)	22.2 / 25.1

The structure of Adp Bound to K114BD Mutant Atp-Grasp Fold of Blastocystis Hominis Succinyl-Coa Synthetase also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Adp Bound to K114BD Mutant Atp-Grasp Fold of Blastocystis Hominis Succinyl-Coa Synthetase (pdb code 6no2). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Adp Bound to K114BD Mutant Atp-Grasp Fold of Blastocystis Hominis Succinyl-Coa Synthetase, PDB code: 6no2:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Adp Bound to K114BD Mutant Atp-Grasp Fold of Blastocystis Hominis Succinyl-Coa Synthetase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Adp Bound to K114BD Mutant Atp-Grasp Fold of Blastocystis Hominis Succinyl-Coa Synthetase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:69.9 occ:1.00 HOA2 A:ADP301 1.9 0.4 0.9 OD2 A:ASP228 2.1 72.9 1.0 O3B A:ADP301 2.2 82.4 0.8 HOB3 A:ADP301 2.3 98.9 0.8 O A:ASN210 2.4 34.8 1.0 O2A A:ADP301 2.6 85.3 0.8 PB A:ADP301 3.1 88.4 0.8 CG A:ASP228 3.2 61.3 1.0 O1B A:ADP301 3.4 91.1 0.8 HB3 A:ASP228 3.4 52.7 1.0 O3A A:ADP301 3.4 86.2 0.8 PA A:ADP301 3.5 84.2 0.8 HB2 A:ASP228 3.5 52.7 1.0 HB3 A:ASN210 3.6 55.1 1.0 CB A:ASP228 3.6 43.9 1.0 C A:ASN210 3.6 32.2 1.0 HD3 A:PRO211 3.8 41.9 1.0 O1A A:ADP301 4.0 86.4 0.8 HD22 A:ASN210 4.1 61.1 1.0 HH21 A:ARG58 4.1 90.0 1.0 OD1 A:ASP228 4.3 67.4 1.0 ND2 A:ASN210 4.3 50.9 1.0 CB A:ASN210 4.3 45.9 1.0 CG A:ASN210 4.4 50.1 1.0 HD2 A:PRO211 4.4 41.9 1.0 CD A:PRO211 4.4 34.9 1.0 O2B A:ADP301 4.5 90.5 0.8 N A:PRO211 4.5 32.8 1.0 CA A:ASN210 4.5 36.4 1.0 HD21 A:ASN210 4.7 61.1 1.0 HOB2 A:ADP301 4.7 0.6 0.9 H A:ASN210 4.7 44.6 1.0 O5' A:ADP301 4.9 78.7 0.8 NH2 A:ARG58 4.9 75.0 1.0 HE A:ARG58 5.0 99.4 1.0 H5'2 A:ADP301 5.0 90.2 0.8

Magnesium binding site 2 out of 2 in the Adp Bound to K114BD Mutant Atp-Grasp Fold of Blastocystis Hominis Succinyl-Coa Synthetase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Adp Bound to K114BD Mutant Atp-Grasp Fold of Blastocystis Hominis Succinyl-Coa Synthetase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:62.5 occ:1.00 HOA2 B:ADP301 1.9 1.0 0.8 OD2 B:ASP228 2.1 76.5 1.0 O2A B:ADP301 2.3 0.1 0.8 O B:ASN210 2.4 34.3 1.0 O3B B:ADP301 2.9 0.4 0.8 PA B:ADP301 3.2 0.8 0.8 CG B:ASP228 3.2 68.0 1.0 HOB3 B:ADP301 3.2 0.7 0.8 O1B B:ADP301 3.4 0.7 0.8 PB B:ADP301 3.4 0.0 0.8 O3A B:ADP301 3.5 0.5 0.8 HB3 B:ASP228 3.5 63.0 1.0 O1A B:ADP301 3.5 0.2 0.8 HB2 B:ASP228 3.6 63.0 1.0 HB3 B:ASN210 3.6 48.3 1.0 CB B:ASP228 3.6 52.5 1.0 C B:ASN210 3.7 31.3 1.0 HD3 B:PRO211 3.9 44.2 1.0 HD22 B:ASN210 4.1 60.4 1.0 OD1 B:ASP228 4.3 73.4 1.0 HH21 B:ARG58 4.3 0.2 1.0 ND2 B:ASN210 4.3 50.3 1.0 CB B:ASN210 4.3 40.2 1.0 CG B:ASN210 4.4 49.0 1.0 CD B:PRO211 4.5 36.8 1.0 HD2 B:PRO211 4.5 44.2 1.0 N B:PRO211 4.5 37.4 1.0 CA B:ASN210 4.6 32.9 1.0 O5' B:ADP301 4.6 0.1 0.8 HD21 B:ASN210 4.7 60.4 1.0 H B:ASN210 4.8 39.2 1.0 O2B B:ADP301 4.9 0.4 0.8

J.Huang, V.H.Nguyen, K.A.Hamblin, R.Maytum, M.Van Der Giezen, M.E.Fraser. Atp-Specificity of Succinyl-Coa Synthetase From Blastocystis Hominis. Acta Crystallogr D Struct V. 75 647 2019BIOL.
ISSN: ISSN 2059-7983
PubMed: 31282474
DOI: 10.1107/S2059798319007976