Magnesium in PDB 9qof: E.Coli Seryl-Trna Synthetase (Arm Deletion Mutant) Bound to Sulphamoyl Seryl-Adenylate Analogue

All present enzymatic activity of E.Coli Seryl-Trna Synthetase (Arm Deletion Mutant) Bound to Sulphamoyl Seryl-Adenylate Analogue:
6.1.1.11;

The structure of E.Coli Seryl-Trna Synthetase (Arm Deletion Mutant) Bound to Sulphamoyl Seryl-Adenylate Analogue, PDB code: 9qof was solved by S.Cusack, H.Belrhali, S.Price, R.Leberman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	11.99 / 2.32
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	132.615, 92.901, 171.691, 90, 90, 90
R / Rfree (%)	13 / 16.3

The binding sites of Magnesium atom in the E.Coli Seryl-Trna Synthetase (Arm Deletion Mutant) Bound to Sulphamoyl Seryl-Adenylate Analogue (pdb code 9qof). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the E.Coli Seryl-Trna Synthetase (Arm Deletion Mutant) Bound to Sulphamoyl Seryl-Adenylate Analogue, PDB code: 9qof:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the E.Coli Seryl-Trna Synthetase (Arm Deletion Mutant) Bound to Sulphamoyl Seryl-Adenylate Analogue


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E.Coli Seryl-Trna Synthetase (Arm Deletion Mutant) Bound to Sulphamoyl Seryl-Adenylate Analogue within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:36.1 occ:1.00 O A:HOH658 2.2 30.4 1.0 O2S A:SSA503 2.7 13.9 1.0 OE2 A:GLU355 2.7 25.1 1.0 O A:HOH732 2.8 43.3 1.0 O A:HOH696 3.3 41.1 1.0 OE1 A:GLU355 3.4 29.6 1.0 CD A:GLU355 3.4 30.6 1.0 HB2 A:SER358 3.6 24.6 1.0 S1 A:SSA503 4.0 18.6 1.0 OG A:SER358 4.1 30.1 1.0 CB A:SER358 4.2 20.5 1.0 HB3 A:SER358 4.3 24.6 1.0 HG A:SER358 4.4 36.1 1.0 O1S A:SSA503 4.4 16.3 1.0 O A:HOH708 4.5 28.1 1.0 OD2 A:ASP342 4.6 24.4 1.0 O3' A:SSA503 4.7 17.9 1.0 CG A:GLU355 4.9 26.3 1.0 O5' A:SSA503 4.9 21.3 1.0 N8 A:SSA503 4.9 16.3 1.0 C3' A:SSA503 5.0 17.6 1.0 OD1 A:ASP342 5.0 20.0 1.0

Magnesium binding site 2 out of 2 in the E.Coli Seryl-Trna Synthetase (Arm Deletion Mutant) Bound to Sulphamoyl Seryl-Adenylate Analogue


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of E.Coli Seryl-Trna Synthetase (Arm Deletion Mutant) Bound to Sulphamoyl Seryl-Adenylate Analogue within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:49.0 occ:1.00 O B:HOH704 2.3 43.5 1.0 O B:HOH721 2.7 42.6 1.0 O2S B:SSA503 2.8 25.7 1.0 OE2 B:GLU355 2.9 33.6 1.0 OE1 B:GLU355 3.3 37.1 1.0 O B:HOH609 3.4 50.9 1.0 CD B:GLU355 3.5 35.6 1.0 S1 B:SSA503 4.1 24.7 1.0 HB2 B:SER358 4.2 26.8 1.0 HG B:SER358 4.2 39.7 1.0 O B:HOH697 4.2 48.6 1.0 O1S B:SSA503 4.3 19.5 1.0 OG B:SER358 4.7 33.1 1.0 O3' B:SSA503 4.7 24.0 1.0 CB B:SER358 4.8 22.3 1.0 O5' B:SSA503 4.8 24.5 1.0 C3' B:SSA503 4.9 21.6 1.0 OD2 B:ASP342 4.9 28.3 1.0 O1 B:SO4502 4.9 77.3 1.0 CG B:GLU355 5.0 33.0 1.0 HB3 B:SER358 5.0 26.8 1.0

F.Borel, C.Vincent, R.Leberman, M.Hartlein. Seryl-Trna Synthetase From Escherichia Coli,Implication of Its N-Terminal Domain in Aminoacylation Activity and Specificity. Nucleic Acids Res V. 22 2963 1994.
ISSN: ISSN 0305-1048
PubMed: 8065908
DOI: 10.1093/NAR/22.15.2963