Magnesium in PDB 1ozf: The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors

All present enzymatic activity of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors:
4.1.3.18;

The structure of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors, PDB code: 1ozf was solved by S.S.Pang, R.G.Duggleby, R.L.Schowen, L.W.Guddat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	100.00 / 2.30
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	116.822, 160.573, 129.374, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 21.4

The binding sites of Magnesium atom in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors (pdb code 1ozf). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors, PDB code: 1ozf:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg699 b:12.6 occ:1.00 O3B A:TPP700 2.0 8.4 1.0 OD1 A:ASP474 2.1 18.5 1.0 O A:GLY476 2.1 16.3 1.0 O A:HOH740 2.1 9.4 1.0 O1A A:TPP700 2.2 8.4 1.0 OD1 A:ASP447 2.3 14.9 1.0 PB A:TPP700 3.0 11.2 1.0 CG A:ASP474 3.1 17.4 1.0 PA A:TPP700 3.1 13.5 1.0 O3A A:TPP700 3.3 11.3 1.0 C A:GLY476 3.3 16.0 1.0 OD2 A:ASP474 3.5 18.1 1.0 CG A:ASP447 3.5 14.9 1.0 O1B A:TPP700 3.5 8.2 1.0 O7 A:TPP700 3.7 14.7 1.0 N A:ASP447 3.9 11.5 1.0 OD2 A:ASP447 4.0 15.4 1.0 N A:GLY476 4.0 16.0 1.0 N A:ASN478 4.0 13.9 1.0 N A:TYR477 4.2 14.6 1.0 CA A:GLY476 4.2 16.4 1.0 N A:GLY448 4.3 10.2 1.0 CA A:TYR477 4.3 14.6 1.0 O2B A:TPP700 4.4 7.6 1.0 CB A:ASP474 4.4 14.5 1.0 O2A A:TPP700 4.5 12.2 1.0 O A:TRP472 4.5 9.8 1.0 CA A:GLY446 4.5 10.4 1.0 N A:ASP474 4.6 12.8 1.0 C A:GLY446 4.6 10.7 1.0 CZ A:PHE496 4.6 10.6 1.0 CB A:ASP447 4.7 11.9 1.0 C A:TYR477 4.7 15.3 1.0 CA A:ASP447 4.7 12.3 1.0 CB A:ASN478 4.8 13.1 1.0 C7 A:TPP700 4.8 16.4 1.0 N A:ASN475 4.9 14.6 1.0 CA A:ASP474 5.0 13.8 1.0

Magnesium binding site 2 out of 2 in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg704 b:15.2 occ:1.00 O3B B:TPP705 2.0 14.8 1.0 O B:HOH706 2.1 15.7 1.0 OD1 B:ASP474 2.1 17.1 1.0 O1A B:TPP705 2.1 16.3 1.0 O B:GLY476 2.2 15.9 1.0 OD1 B:ASP447 2.3 16.1 1.0 CG B:ASP474 3.0 17.5 1.0 PB B:TPP705 3.0 14.4 1.0 PA B:TPP705 3.1 15.1 1.0 O3A B:TPP705 3.2 15.7 1.0 C B:GLY476 3.4 16.2 1.0 OD2 B:ASP474 3.4 18.9 1.0 CG B:ASP447 3.4 16.1 1.0 O1B B:TPP705 3.5 14.8 1.0 O7 B:TPP705 3.7 18.4 1.0 N B:ASP447 3.9 12.8 1.0 OD2 B:ASP447 4.0 15.3 1.0 N B:GLY476 4.0 17.9 1.0 N B:ASN478 4.1 15.9 1.0 N B:TYR477 4.3 17.0 1.0 N B:GLY448 4.3 12.8 1.0 CB B:ASP474 4.3 18.0 1.0 CA B:GLY476 4.3 16.8 1.0 CA B:TYR477 4.3 16.5 1.0 O2B B:TPP705 4.4 14.6 1.0 O2A B:TPP705 4.4 18.0 1.0 CA B:GLY446 4.5 14.1 1.0 O B:TRP472 4.5 14.3 1.0 C B:GLY446 4.6 13.5 1.0 N B:ASP474 4.6 14.8 1.0 CB B:ASP447 4.6 13.8 1.0 CZ B:PHE496 4.7 19.6 1.0 CA B:ASP447 4.7 14.7 1.0 C7 B:TPP705 4.8 21.4 1.0 CB B:ASN478 4.8 14.5 1.0 C B:TYR477 4.8 15.3 1.0 N B:ASN475 4.8 16.4 1.0 CE1 B:TYR543 4.9 14.2 1.0 CA B:ASP474 4.9 15.8 1.0

S.S.Pang, R.G.Duggleby, R.L.Schowen, L.W.Guddat. The Crystal Structures of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate. J.Biol.Chem. V. 279 2242 2004.
ISSN: ISSN 0021-9258
PubMed: 14557277
DOI: 10.1074/JBC.M304038200