Magnesium in PDB 2bhb: Zn Substituted E. Coli Aminopeptidase P

All present enzymatic activity of Zn Substituted E. Coli Aminopeptidase P:
3.4.11.9;

The structure of Zn Substituted E. Coli Aminopeptidase P, PDB code: 2bhb was solved by S.C.Graham, C.S.Bond, H.C.Freeman, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.19 / 2.41
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	138.814, 138.814, 230.914, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 19

The structure of Zn Substituted E. Coli Aminopeptidase P also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

The binding sites of Magnesium atom in the Zn Substituted E. Coli Aminopeptidase P (pdb code 2bhb). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Zn Substituted E. Coli Aminopeptidase P, PDB code: 2bhb:

Magnesium binding site 1 out of 1 in the Zn Substituted E. Coli Aminopeptidase P


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Zn Substituted E. Coli Aminopeptidase P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1003 b:57.0 occ:1.00 O A:HOH2211 2.2 56.5 1.0 O A:HOH2216 2.2 56.5 1.0 O A:HOH2212 2.2 55.2 1.0 O A:HOH2214 2.2 55.1 1.0 O A:HOH2213 2.2 56.4 1.0 O A:HOH2215 2.2 57.5 1.0 O A:ARG399 3.8 45.2 1.0 OE2 A:GLU396 4.0 48.4 1.0 O A:GLN397 4.3 45.8 1.0 O A:GLU396 4.6 42.1 1.0 O A:HOH2151 4.6 56.4 1.0 O A:HOH2191 4.8 41.6 1.0 O A:HOH2127 4.8 54.3 1.0 C A:GLN397 4.8 44.5 1.0 CD A:GLU396 4.9 48.1 1.0 C A:ARG399 5.0 45.2 1.0

S.C.Graham, C.S.Bond, H.C.Freeman, J.M.Guss. Structural and Functional Implications of Metal Ion Selection in Aminopeptidase P, A Metalloprotease with A Dinuclear Metal Center. Biochemistry V. 44 13820 2005.
ISSN: ISSN 0006-2960
PubMed: 16229471
DOI: 10.1021/BI0512849