Magnesium in PDB 2alm: Crystal Structure Analysis of A Mutant Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae

All present enzymatic activity of Crystal Structure Analysis of A Mutant Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae:
2.3.1.41;

The structure of Crystal Structure Analysis of A Mutant Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, PDB code: 2alm was solved by Y.M.Zhang, J.Hurlbert, S.W.White, C.O.Rock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.60
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	60.393, 88.820, 61.048, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 25.7

The binding sites of Magnesium atom in the Crystal Structure Analysis of A Mutant Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae (pdb code 2alm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure Analysis of A Mutant Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, PDB code: 2alm:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure Analysis of A Mutant Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure Analysis of A Mutant Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:40.0 occ:1.00 O A:ASN392 2.6 34.3 1.0 O A:ASN301 2.7 35.1 1.0 OE1 A:GLU346 2.8 44.2 1.0 OD1 A:ASN301 2.8 34.3 1.0 OG A:SER391 2.9 31.8 1.0 O A:ALA302 3.2 37.5 1.0 N A:ASN392 3.4 34.0 1.0 CD A:GLU346 3.5 42.7 1.0 C A:ASN301 3.6 33.9 1.0 C A:ALA302 3.6 36.5 1.0 CG A:GLU346 3.6 41.1 1.0 C A:ASN392 3.6 34.5 1.0 CB A:GLU346 3.6 38.5 1.0 CG A:ASN301 3.7 33.0 1.0 C A:SER391 3.9 34.2 1.0 N A:ALA303 4.0 37.3 1.0 CB A:ASN301 4.0 33.2 1.0 CB A:SER391 4.0 31.4 1.0 CA A:ASN392 4.0 33.8 1.0 CA A:SER391 4.1 33.4 1.0 CA A:ALA303 4.1 38.3 1.0 N A:ALA302 4.3 34.9 1.0 CA A:ALA302 4.3 34.9 1.0 CG2 A:THR393 4.4 33.9 1.0 CA A:ASN301 4.4 32.5 1.0 OE2 A:GLU346 4.7 45.2 1.0 NZ A:LYS332 4.8 34.2 1.0 O A:SER391 4.8 35.5 1.0 N A:THR393 4.8 34.5 1.0 ND2 A:ASN301 4.9 33.1 1.0 O A:HOH504 4.9 30.1 1.0 CB A:ASN392 4.9 35.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure Analysis of A Mutant Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure Analysis of A Mutant Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:35.6 occ:1.00 O A:ALA218 2.7 37.6 1.0 N A:ASN227 2.8 37.6 1.0 ND2 A:ASN227 2.8 34.6 1.0 O A:GLY228 2.9 34.9 1.0 O A:HOH539 2.9 48.4 1.0 OG A:SER306 2.9 36.9 1.0 N A:GLY228 3.4 35.6 1.0 CA A:ARG226 3.4 38.1 1.0 O A:SER306 3.5 39.8 1.0 C A:ARG226 3.6 37.9 1.0 C A:ALA218 3.8 36.0 1.0 CA A:ASN227 3.8 37.4 1.0 CB A:ARG226 3.9 38.3 1.0 C A:ASN227 3.9 37.3 1.0 C A:GLY228 3.9 35.0 1.0 CB A:SER210 3.9 37.5 1.0 CG1 A:ILE220 4.0 30.2 1.0 CB A:SER306 4.0 39.2 1.0 OG A:SER210 4.0 39.7 1.0 CG A:ASN227 4.0 35.8 1.0 N A:ILE220 4.2 34.5 1.0 CA A:GLY228 4.2 34.1 1.0 C A:SER306 4.5 39.5 1.0 O A:ARG217 4.5 37.4 1.0 CA A:SER219 4.5 34.9 1.0 CB A:ASN227 4.5 36.4 1.0 N A:SER219 4.6 35.7 1.0 CD1 A:ILE220 4.6 29.6 1.0 O A:ASP225 4.7 40.9 1.0 N A:ARG226 4.7 38.4 1.0 O A:ARG226 4.8 36.8 1.0 CA A:ALA218 4.8 34.9 1.0 CA A:SER306 4.8 39.9 1.0 O A:ASN227 4.8 39.4 1.0 C A:SER219 4.9 35.5 1.0 OD1 A:ASN227 5.0 34.8 1.0

Y.M.Zhang, J.Hurlbert, S.W.White, C.O.Rock. Roles of the Active Site Water, Histidine 303, and Phenylalanine 396 in the Catalytic Mechanism of the Elongation Condensing Enzyme of Streptococcus Pneumoniae. J.Biol.Chem. V. 281 17390 2006.
ISSN: ISSN 0021-9258
PubMed: 16618705
DOI: 10.1074/JBC.M513199200