Manganese in PDB 2bn7: Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn

All present enzymatic activity of Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn:
3.4.11.9;

The structure of Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn, PDB code: 2bn7 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)	119.52 / 2.40
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	139.695, 139.695, 230.674, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 18.7

The structure of Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Zinc	(Zn)	1 atom

The binding sites of Manganese atom in the Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn (pdb code 2bn7). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn, PDB code: 2bn7:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1441 b:41.9 occ:1.00 O A:HOH2284 2.0 42.8 1.0 OE2 A:GLU406 2.1 53.4 1.0 NE2 A:HIS354 2.2 52.6 1.0 OD2 A:ASP271 2.2 52.6 1.0 OE2 A:GLU383 2.4 58.8 1.0 CD A:GLU406 3.1 52.8 1.0 CE1 A:HIS354 3.1 51.0 1.0 CD A:GLU383 3.1 54.4 1.0 CD2 A:HIS354 3.1 52.1 1.0 MN A:MN1442 3.1 47.3 1.0 CG A:ASP271 3.1 53.7 1.0 OE1 A:GLU383 3.3 54.2 1.0 OE1 A:GLU406 3.4 52.1 1.0 OD1 A:ASP271 3.5 58.5 1.0 CG2 A:THR381 3.6 50.7 1.0 OG1 A:THR381 3.8 49.3 1.0 CB A:THR381 3.9 51.9 1.0 ND1 A:HIS354 4.2 49.4 1.0 CG A:HIS354 4.2 49.4 1.0 O A:HOH2286 4.3 58.6 1.0 N A:PRO501 4.3 53.8 1.0 CG A:GLU406 4.4 52.6 1.0 CB A:ASP271 4.4 53.1 1.0 CG A:GLU383 4.4 53.9 1.0 CA A:PRO501 4.5 54.1 1.0 NE2 A:HIS361 4.7 56.5 1.0 O A:HOH2228 4.8 41.4 1.0 CD2 A:HIS361 4.9 56.6 1.0 ZN A:ZN1445 4.9 70.4 0.8

Manganese binding site 2 out of 2 in the Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Mn Substituted E. Coli Aminopeptidase P in Complex with Product and Zn within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1442 b:47.3 occ:1.00 OD1 A:ASP271 2.1 58.5 1.0 OE1 A:GLU406 2.1 52.1 1.0 OD1 A:ASP260 2.2 53.7 1.0 O A:HOH2284 2.2 42.8 1.0 OD2 A:ASP260 2.4 55.6 1.0 CG A:ASP260 2.6 53.5 1.0 CD A:GLU406 3.0 52.8 1.0 CG A:ASP271 3.0 53.7 1.0 MN A:MN1441 3.1 41.9 1.0 OE2 A:GLU406 3.2 53.4 1.0 OD2 A:ASP271 3.2 52.6 1.0 O A:HOH2286 3.3 58.6 1.0 OG1 A:THR273 3.6 50.2 1.0 OH A:TYR229 3.7 48.6 1.0 OE1 A:GLU383 4.1 54.2 1.0 CB A:ASP260 4.1 52.2 1.0 CZ A:TYR229 4.2 49.0 1.0 CG A:GLU406 4.3 52.6 1.0 CB A:ASP271 4.4 53.1 1.0 N A:PRO501 4.5 53.8 1.0 CE2 A:TYR229 4.5 48.5 1.0 C A:ASP271 4.6 52.8 1.0 O A:ILE272 4.6 50.8 1.0 CD A:GLU383 4.7 54.4 1.0 O A:ASP271 4.8 52.6 1.0 C A:ILE272 4.8 50.9 1.0 N A:ILE272 4.8 51.9 1.0 CA A:ASP271 4.8 52.6 1.0 OE2 A:GLU383 4.8 58.8 1.0 CD A:PRO501 4.8 53.3 1.0 NE A:ARG404 4.8 51.9 1.0 CA A:ASP260 4.9 52.6 1.0 CB A:GLU406 4.9 53.1 1.0 CE1 A:TYR229 5.0 49.1 1.0 CB A:THR273 5.0 49.6 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