Magnesium in PDB 1wl6: Mg-Substituted Form of E. Coli Aminopeptidase P

All present enzymatic activity of Mg-Substituted Form of E. Coli Aminopeptidase P:
3.4.11.9;

The structure of Mg-Substituted Form of E. Coli Aminopeptidase P, PDB code: 1wl6 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)	42.26 / 2.00
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	177.733, 177.733, 96.484, 90.00, 90.00, 120.00
R / Rfree (%)	14.8 / 17.3

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

Chlorine

(Cl)

2 atoms

The binding sites of Magnesium atom in the Mg-Substituted Form of E. Coli Aminopeptidase P (pdb code 1wl6). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Mg-Substituted Form of E. Coli Aminopeptidase P, PDB code: 1wl6:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Mg-Substituted Form of 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 Mg-Substituted Form of E. Coli Aminopeptidase P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg801 b:17.1 occ:1.00 OE2 A:GLU406 2.1 16.8 1.0 O A:HOH904 2.1 20.1 1.0 OD2 A:ASP271 2.1 15.3 1.0 NE2 A:HIS354 2.2 14.2 1.0 OE2 A:GLU383 2.2 15.5 1.0 O A:HOH1083 2.3 28.1 1.0 CD A:GLU383 3.0 17.8 1.0 CG A:ASP271 3.0 16.0 1.0 OE1 A:GLU383 3.1 17.6 1.0 CD A:GLU406 3.1 14.4 1.0 CD2 A:HIS354 3.1 14.6 1.0 CE1 A:HIS354 3.2 15.2 1.0 MG A:MG802 3.3 20.2 1.0 OD1 A:ASP271 3.4 15.4 1.0 OE1 A:GLU406 3.5 16.0 1.0 O A:HOH1245 3.9 21.3 1.0 OG1 A:THR381 4.0 12.4 1.0 CG2 A:THR381 4.0 12.7 1.0 O2 A:IPA902 4.1 30.0 1.0 CB A:THR381 4.3 13.6 1.0 CB A:ASP271 4.3 14.6 1.0 ND1 A:HIS354 4.3 13.3 1.0 CG A:HIS354 4.3 11.8 1.0 CG A:GLU383 4.3 15.5 1.0 CG A:GLU406 4.4 14.4 1.0 NE2 A:HIS361 4.6 18.6 1.0 O A:HOH1006 4.8 25.0 1.0 CD2 A:HIS361 4.9 22.2 1.0 C1 A:IPA902 4.9 28.3 1.0

Magnesium binding site 2 out of 2 in the Mg-Substituted Form of E. Coli Aminopeptidase P


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Mg-Substituted Form of E. Coli Aminopeptidase P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg802 b:20.2 occ:1.00 OD1 A:ASP271 2.0 15.4 1.0 O A:HOH904 2.0 20.1 1.0 OE1 A:GLU406 2.1 16.0 1.0 OD1 A:ASP260 2.1 13.1 1.0 O A:HOH1245 2.2 21.3 1.0 OD2 A:ASP260 2.3 12.3 1.0 CG A:ASP260 2.5 13.9 1.0 CG A:ASP271 3.0 16.0 1.0 CD A:GLU406 3.0 14.4 1.0 OE2 A:GLU406 3.2 16.8 1.0 OD2 A:ASP271 3.2 15.3 1.0 MG A:MG801 3.3 17.1 1.0 OG1 A:THR273 3.5 13.5 1.0 OH A:TYR229 3.7 14.7 1.0 OE1 A:GLU383 3.9 17.6 1.0 CB A:ASP260 4.0 12.0 1.0 O A:HOH1083 4.2 28.1 1.0 CZ A:TYR229 4.2 11.7 1.0 O2 A:IPA902 4.4 30.0 1.0 CB A:ASP271 4.4 14.6 1.0 CG A:GLU406 4.4 14.4 1.0 CE2 A:TYR229 4.5 15.4 1.0 C A:ASP271 4.6 13.9 1.0 O A:ILE272 4.6 15.6 1.0 CD A:GLU383 4.7 17.8 1.0 NE A:ARG404 4.7 13.2 1.0 CA A:ASP271 4.7 12.9 1.0 OE2 A:GLU383 4.7 15.5 1.0 N A:ILE272 4.8 12.1 1.0 C A:ILE272 4.8 13.3 1.0 CA A:ASP260 4.8 13.0 1.0 O A:ASP271 4.9 14.1 1.0 CE1 A:TYR229 4.9 14.2 1.0 CB A:GLU406 4.9 13.4 1.0 CB A:THR273 4.9 12.8 1.0 NH2 A:ARG404 5.0 13.7 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