Magnesium in PDB 3rmj: Crystal Structure of Truncated Alpha-Isopropylmalate Synthase From Neisseria Meningitidis

All present enzymatic activity of Crystal Structure of Truncated Alpha-Isopropylmalate Synthase From Neisseria Meningitidis:
2.3.3.13;

The structure of Crystal Structure of Truncated Alpha-Isopropylmalate Synthase From Neisseria Meningitidis, PDB code: 3rmj was solved by F.H.A.Huisman, H.M.Baker, N.Koon, E.N.Baker, E.J.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.81 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.296, 103.581, 129.937, 90.00, 90.00, 90.00
R / Rfree (%)	15.8 / 19.1

The structure of Crystal Structure of Truncated Alpha-Isopropylmalate Synthase From Neisseria Meningitidis also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Truncated Alpha-Isopropylmalate Synthase From Neisseria Meningitidis (pdb code 3rmj). 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 of Truncated Alpha-Isopropylmalate Synthase From Neisseria Meningitidis, PDB code: 3rmj:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Truncated Alpha-Isopropylmalate Synthase From Neisseria Meningitidis


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 Truncated Alpha-Isopropylmalate Synthase From Neisseria Meningitidis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg366 b:43.8 occ:1.00 O A:HOH492 1.9 26.3 1.0 O A:ILE278 2.0 34.9 1.0 O A:HOH495 2.0 38.0 1.0 O A:HOH491 2.2 32.9 1.0 O A:HOH493 2.3 31.2 1.0 O A:HOH494 2.3 39.3 1.0 C A:ILE278 3.2 33.1 1.0 CA A:THR279 3.9 27.9 1.0 OE2 A:GLU29 4.0 23.0 1.0 N A:THR279 4.0 29.6 1.0 O A:ALA24 4.1 22.0 1.0 OE1 A:GLU29 4.1 21.6 1.0 CA A:ILE278 4.3 32.4 1.0 C A:THR279 4.3 29.9 1.0 CG2 A:ILE278 4.3 31.5 1.0 CD A:GLU29 4.4 22.8 1.0 O A:THR279 4.6 32.1 1.0 O A:GLY22 4.7 24.2 1.0 N A:GLY280 4.9 28.9 1.0 CB A:ILE278 5.0 31.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Truncated Alpha-Isopropylmalate Synthase From Neisseria Meningitidis


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 Truncated Alpha-Isopropylmalate Synthase From Neisseria Meningitidis within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg366 b:47.6 occ:1.00 O B:HOH482 2.1 34.6 1.0 O B:HOH479 2.1 30.9 1.0 O B:ALA24 2.1 25.2 1.0 O B:HOH483 2.2 35.8 1.0 O B:HOH480 2.2 33.9 1.0 O B:HOH481 2.3 31.9 1.0 C B:ALA24 3.4 24.3 1.0 O B:ILE278 4.1 25.3 1.0 OE1 B:GLU29 4.1 24.7 1.0 O B:GLY22 4.2 24.2 1.0 CA B:MET25 4.2 23.8 1.0 O B:HOH526 4.2 27.2 1.0 N B:MET25 4.2 23.3 1.0 O B:HOH500 4.2 31.9 1.0 O B:HOH524 4.3 31.2 1.0 O B:HOH484 4.3 36.4 1.0 CA B:ALA24 4.4 23.3 1.0 O B:HOH528 4.4 45.9 1.0 N B:ALA24 4.4 21.4 1.0 C B:ALA23 4.5 22.4 1.0 O B:ALA23 4.6 21.9 1.0 CB B:ALA24 4.8 23.9 1.0 CG B:MET25 4.9 23.5 1.0 OE2 B:GLU29 4.9 26.8 1.0 CD B:GLU29 5.0 24.8 1.0

F.H.A.Huisman, N.Koon, E.M.M.Bulloch, H.M.Baker, E.N.Baker, C.J.Squire, E.J.Parker. Removal of the C-Terminal Regulatory Domain of Alpha-Isopropylmalate Synthase Disrupts Functional Substrate Binding Biochemistry V. 51 2289 2012.
ISSN: ISSN 0006-2960
PubMed: 22352945
DOI: 10.1021/BI201717J