Manganese in PDB 1wl9: Structure of Aminopeptidase P From E. Coli

All present enzymatic activity of Structure of Aminopeptidase P From E. Coli:
3.4.11.9;

The structure of Structure of Aminopeptidase P From E. Coli, PDB code: 1wl9 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)	38.35 / 1.90
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	177.420, 177.420, 96.420, 90.00, 90.00, 120.00
R / Rfree (%)	15.2 / 17

The structure of Structure of Aminopeptidase P From E. Coli also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Manganese atom in the Structure of Aminopeptidase P From E. Coli (pdb code 1wl9). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Aminopeptidase P From E. Coli, PDB code: 1wl9:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of Aminopeptidase P From E. Coli


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Aminopeptidase P From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1001 b:18.1 occ:1.00 O A:HOH1004 2.0 16.9 1.0 OE2 A:GLU406 2.1 15.5 1.0 NE2 A:HIS354 2.2 12.4 1.0 OD2 A:ASP271 2.2 14.2 1.0 OE2 A:GLU383 2.3 19.3 1.0 O A:HOH1070 2.8 30.2 1.0 CD A:GLU383 3.0 18.0 1.0 CG A:ASP271 3.1 14.2 1.0 CD2 A:HIS354 3.1 12.7 1.0 CD A:GLU406 3.2 14.3 1.0 CE1 A:HIS354 3.2 12.3 1.0 OE1 A:GLU383 3.2 18.4 1.0 MN A:MN1002 3.3 18.6 1.0 OD1 A:ASP271 3.5 14.8 1.0 OE1 A:GLU406 3.5 14.1 1.0 O A:HOH1559 3.8 22.8 1.0 CG2 A:THR381 3.8 12.5 1.0 OG1 A:THR381 3.8 13.0 1.0 CB A:THR381 4.1 13.5 1.0 CG A:HIS354 4.3 13.0 1.0 ND1 A:HIS354 4.3 13.1 1.0 CG A:GLU383 4.4 16.0 1.0 CB A:ASP271 4.4 13.5 1.0 CG A:GLU406 4.5 12.4 1.0 NE2 A:HIS361 4.8 16.5 1.0 CG2 A:VAL360 4.9 16.0 1.0 O A:HOH1349 4.9 33.2 1.0 CD2 A:HIS361 5.0 17.7 1.0

Manganese binding site 2 out of 2 in the Structure of Aminopeptidase P From E. Coli


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Aminopeptidase P From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1002 b:18.6 occ:1.00 OD1 A:ASP271 2.1 14.8 1.0 O A:HOH1004 2.1 16.9 1.0 OD1 A:ASP260 2.2 11.1 1.0 OE1 A:GLU406 2.2 14.1 1.0 OD2 A:ASP260 2.3 11.3 1.0 O A:HOH1559 2.4 22.8 1.0 CG A:ASP260 2.6 14.3 1.0 CD A:GLU406 3.1 14.3 1.0 CG A:ASP271 3.1 14.2 1.0 OE2 A:GLU406 3.3 15.5 1.0 MN A:MN1001 3.3 18.1 1.0 OD2 A:ASP271 3.4 14.2 1.0 OG1 A:THR273 3.5 12.3 1.0 OH A:TYR229 3.7 13.5 1.0 OE1 A:GLU383 4.0 18.4 1.0 CB A:ASP260 4.1 14.0 1.0 O A:HOH1070 4.1 30.2 1.0 CZ A:TYR229 4.1 13.2 1.0 CG A:GLU406 4.4 12.4 1.0 CB A:ASP271 4.4 13.5 1.0 O A:HOH1533 4.5 45.2 1.0 CE2 A:TYR229 4.5 14.4 1.0 C A:ASP271 4.6 13.2 1.0 O A:ILE272 4.7 13.8 1.0 CD A:GLU383 4.7 18.0 1.0 NE A:ARG404 4.7 15.6 1.0 N A:ILE272 4.8 13.2 1.0 C A:ILE272 4.8 13.1 1.0 CA A:ASP271 4.8 12.6 1.0 OE2 A:GLU383 4.8 19.3 1.0 O A:ASP271 4.8 11.1 1.0 CE1 A:TYR229 4.8 14.0 1.0 CA A:ASP260 4.9 13.2 1.0 CB A:THR273 4.9 11.4 1.0 N A:THR273 5.0 12.7 1.0 NH2 A:ARG404 5.0 15.9 1.0 CB A:GLU406 5.0 11.2 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