Manganese 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:

Magnesium

(Mg)

2 atoms

The binding sites of Manganese 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 Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Truncated Alpha-Isopropylmalate Synthase From Neisseria Meningitidis, PDB code: 3rmj:
Jump to Manganese binding site number: 1; 2;

Manganese 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 Manganese with other atoms in the Mn 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:Mn365 b:22.5 occ:1.00 O A:HOH369 2.1 15.2 1.0 OD1 A:ASN240 2.1 13.9 1.0 OD2 A:ASP16 2.2 17.9 1.0 NE2 A:HIS204 2.2 14.8 1.0 NE2 A:HIS206 2.2 12.8 1.0 O A:HOH497 2.2 19.1 1.0 CD2 A:HIS206 3.0 13.0 1.0 CE1 A:HIS204 3.0 15.9 1.0 CG A:ASN240 3.1 14.8 1.0 CG A:ASP16 3.1 17.9 1.0 CD2 A:HIS204 3.2 14.5 1.0 CE1 A:HIS206 3.3 13.9 1.0 OD1 A:ASP16 3.5 19.5 1.0 ND2 A:ASN240 3.5 15.7 1.0 O A:HOH488 4.1 33.2 1.0 O A:HOH469 4.2 22.1 1.0 ND1 A:HIS204 4.2 16.4 1.0 CG A:HIS206 4.2 12.7 1.0 O A:HOH425 4.3 22.5 1.0 CG A:HIS204 4.3 13.8 1.0 ND1 A:HIS206 4.3 14.2 1.0 O A:HOH370 4.4 13.9 1.0 CB A:ASP16 4.4 16.4 1.0 CB A:ASN240 4.5 14.3 1.0

Manganese 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 Manganese with other atoms in the Mn 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:Mn365 b:24.7 occ:1.00 OD2 B:ASP16 2.1 18.3 1.0 NE2 B:HIS206 2.1 15.5 1.0 OD1 B:ASN240 2.1 15.8 1.0 O B:HOH370 2.2 17.4 1.0 NE2 B:HIS204 2.2 15.3 1.0 O B:HOH421 2.3 17.2 1.0 CD2 B:HIS206 3.0 14.8 1.0 CG B:ASN240 3.1 16.8 1.0 CG B:ASP16 3.1 17.9 1.0 CE1 B:HIS206 3.2 15.4 1.0 CD2 B:HIS204 3.2 15.1 1.0 CE1 B:HIS204 3.2 17.3 1.0 ND2 B:ASN240 3.4 17.2 1.0 OD1 B:ASP16 3.5 19.7 1.0 O B:HOH457 4.2 27.4 1.0 CG B:HIS206 4.2 15.3 1.0 ND1 B:HIS206 4.2 16.4 1.0 O B:HOH376 4.3 23.7 1.0 O B:HOH418 4.4 22.8 1.0 CG B:HIS204 4.4 14.9 1.0 ND1 B:HIS204 4.4 16.2 1.0 CB B:ASP16 4.4 18.0 1.0 CB B:ASN240 4.4 15.0 1.0 CA B:ASN240 5.0 15.0 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