Manganese in PDB 3iu7: M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02

All present enzymatic activity of M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02:
3.4.11.18;

The structure of M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02, PDB code: 3iu7 was solved by Q.Z.Ye, J.P.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.14 / 1.40
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	106.412, 106.412, 50.422, 90.00, 90.00, 120.00
R / Rfree (%)	17.1 / 19

The structure of M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02 also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Manganese atom in the M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02 (pdb code 3iu7). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02, PDB code: 3iu7:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn286 b:6.8 occ:1.00 OD2 A:ASP142 2.1 7.0 1.0 OXT A:FCD288 2.1 7.8 1.0 OD1 A:ASP131 2.2 7.8 1.0 OE2 A:GLU269 2.2 7.4 1.0 O A:HOH539 2.3 8.0 1.0 OD2 A:ASP131 2.3 7.7 1.0 CG A:ASP131 2.6 7.4 1.0 CG A:ASP142 3.1 5.8 1.0 CD A:GLU269 3.1 5.9 1.0 C A:FCD288 3.2 8.3 1.0 OE1 A:GLU269 3.3 6.9 1.0 OD1 A:ASP142 3.3 6.2 1.0 MN A:MN287 3.5 6.7 1.0 CB A:FCD288 3.8 10.6 1.0 CA A:FCD288 3.8 9.8 1.0 OG1 A:THR133 3.9 7.3 1.0 CB A:ASP131 4.1 6.6 1.0 OB A:FCD288 4.2 9.8 1.0 ND2 A:ASN144 4.2 6.2 1.0 O A:HOH331 4.2 10.6 1.0 OE1 A:GLU238 4.4 11.2 1.0 CB A:ASP142 4.4 6.4 1.0 CG A:GLU269 4.4 6.5 1.0 N A:THR143 4.5 5.1 1.0 O A:THR143 4.6 6.7 1.0 O A:HOH351 4.6 8.0 1.0 C A:ASP142 4.7 5.0 1.0 CB A:ASN144 4.7 6.6 1.0 C A:THR143 4.8 5.9 1.0 CA A:ASP131 4.8 5.9 1.0 O A:HOH410 4.8 11.8 1.0 CA A:ASP142 4.8 4.8 1.0 O A:VAL132 4.8 7.5 1.0 C A:ASP131 4.9 5.3 1.0 N A:VAL132 4.9 6.5 1.0

Manganese binding site 2 out of 2 in the M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of M. Tuberculosis Methionine Aminopeptidase with Mn Inhibitor A02 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn287 b:6.7 occ:1.00 OE1 A:GLU269 2.2 6.9 1.0 OE2 A:GLU238 2.2 6.6 1.0 NE2 A:HIS205 2.2 6.4 1.0 OD1 A:ASP142 2.2 6.2 1.0 OXT A:FCD288 2.2 7.8 1.0 OB A:FCD288 2.4 9.8 1.0 C A:FCD288 2.7 8.3 1.0 CD A:GLU238 3.0 7.1 1.0 CD2 A:HIS205 3.1 5.8 1.0 OE1 A:GLU238 3.1 11.2 1.0 CG A:ASP142 3.2 5.8 1.0 CD A:GLU269 3.2 5.9 1.0 CE1 A:HIS205 3.2 5.9 1.0 MN A:MN286 3.5 6.8 1.0 OD2 A:ASP142 3.6 7.0 1.0 OE2 A:GLU269 3.6 7.4 1.0 OG1 A:THR236 3.9 6.1 1.0 CG2 A:THR236 3.9 7.3 1.0 CA A:FCD288 4.1 9.8 1.0 CB A:THR236 4.2 5.8 1.0 CG A:HIS205 4.3 5.2 1.0 CB A:ASP142 4.3 6.4 1.0 ND1 A:HIS205 4.4 6.1 1.0 CG A:GLU238 4.4 7.3 1.0 CG A:GLU269 4.4 6.5 1.0 NE2 A:HIS212 4.5 9.8 1.0 O A:HOH410 4.6 11.8 1.0 CE1 A:PHE211 4.7 7.8 1.0 O A:HOH539 4.7 8.0 1.0 CD2 A:HIS212 5.0 7.7 1.0 OA A:FCD288 5.0 8.6 1.0 O A:HOH503 5.0 26.9 1.0 CB A:GLU238 5.0 6.9 1.0

J.P.Lu, S.C.Chai, Q.Z.Ye. Catalysis and Inhibition of Mycobacterium Tuberculosis Methionine Aminopeptidase J.Med.Chem. V. 53 1329 2010.
ISSN: ISSN 0022-2623
PubMed: 20038112
DOI: 10.1021/JM901624N