Manganese in PDB 2q96: E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A18

All present enzymatic activity of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A18:
3.4.11.18;

The structure of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A18, PDB code: 2q96 was solved by Q.-Z.Ye, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.94 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	39.285, 62.028, 52.426, 90.00, 108.76, 90.00
R / Rfree (%)	21.1 / 23.5

The structure of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A18 also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Sodium	(Na)	1 atom

The binding sites of Manganese atom in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A18 (pdb code 2q96). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A18, PDB code: 2q96:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A18


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A18 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:8.2 occ:1.00 OE2 A:GLU235 2.1 8.4 1.0 OE2 A:GLU204 2.2 6.4 1.0 OD2 A:ASP108 2.2 7.9 1.0 NE2 A:HIS171 2.2 7.8 1.0 OAN A:A18400 2.2 9.6 1.0 OAO A:A18400 2.4 8.5 1.0 CAE A:A18400 2.6 11.1 1.0 CD A:GLU204 2.9 12.3 1.0 OE1 A:GLU204 3.1 15.8 1.0 CD2 A:HIS171 3.1 9.7 1.0 CD A:GLU235 3.1 7.5 1.0 CG A:ASP108 3.2 7.3 1.0 CE1 A:HIS171 3.3 9.0 1.0 OE1 A:GLU235 3.5 7.8 1.0 MN A:MN302 3.5 8.4 1.0 OD1 A:ASP108 3.7 5.9 1.0 OG1 A:THR202 3.8 7.2 1.0 CAA A:A18400 4.1 11.7 1.0 CG2 A:THR202 4.1 8.5 1.0 CB A:ASP108 4.3 7.7 1.0 CB A:THR202 4.3 6.8 1.0 CG A:HIS171 4.3 7.8 1.0 CG A:GLU204 4.3 10.6 1.0 ND1 A:HIS171 4.3 9.4 1.0 CG A:GLU235 4.5 8.6 1.0 O A:HOH540 4.6 11.5 1.0 NE2 A:HIS178 4.7 11.0 1.0 O A:HOH503 4.7 7.8 1.0 CE1 A:PHE177 4.7 8.0 1.0 CD2 A:HIS178 4.9 11.3 1.0 OAM A:A18400 4.9 11.3 1.0

Manganese binding site 2 out of 2 in the E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A18


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of E. Coli Methionine Aminopeptidase Mn-Form with Inhibitor A18 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn302 b:8.4 occ:1.00 OE1 A:GLU235 2.1 7.8 1.0 OD1 A:ASP108 2.2 5.9 1.0 OAO A:A18400 2.2 8.5 1.0 OD1 A:ASP97 2.2 8.7 1.0 O A:HOH503 2.2 7.8 1.0 OD2 A:ASP97 2.5 6.8 1.0 CG A:ASP97 2.6 5.2 1.0 CG A:ASP108 3.1 7.3 1.0 CD A:GLU235 3.1 7.5 1.0 CAE A:A18400 3.2 11.1 1.0 OD2 A:ASP108 3.3 7.9 1.0 OE2 A:GLU235 3.4 8.4 1.0 MN A:MN301 3.5 8.2 1.0 O A:HOH507 3.8 6.9 1.0 OG1 A:THR99 3.8 7.3 1.0 CAA A:A18400 3.9 11.7 1.0 CAB A:A18400 3.9 13.6 1.0 OAN A:A18400 4.1 9.6 1.0 CB A:ASP97 4.1 7.6 1.0 O A:VAL98 4.2 7.9 1.0 OE1 A:GLU204 4.2 15.8 1.0 O A:HOH519 4.3 11.2 1.0 N A:THR109 4.3 7.1 1.0 CB A:ASP108 4.5 7.7 1.0 CG A:GLU235 4.5 8.6 1.0 O A:THR109 4.6 8.0 1.0 C A:THR109 4.7 8.1 1.0 O A:HOH540 4.7 11.5 1.0 O A:HOH555 4.7 12.2 1.0 C A:ASP108 4.7 7.9 1.0 N A:VAL98 4.7 6.5 1.0 CA A:ASP97 4.8 6.6 1.0 CA A:ASP108 4.9 7.2 1.0 C A:VAL98 4.9 6.8 1.0 C A:ASP97 4.9 7.8 1.0 CA A:THR109 4.9 7.0 1.0 CB A:GLU235 4.9 5.3 1.0 CD A:GLU204 4.9 12.3 1.0 CB A:SER110 5.0 6.2 1.0

Z.Q.Ma, S.X.Xie, Q.Q.Huang, F.J.Nan, T.D.Hurley, Q.Z.Ye. Structural Analysis of Inhibition of E. Coli Methionine Aminopeptidase: Implication of Loop Flexibility in Selective Inhibition of Bacterial Enzymes. Bmc Struct.Biol. V. 7 84 2007.
ISSN: ESSN 1472-6807
PubMed: 18093325
DOI: 10.1186/1472-6807-7-84