Manganese in PDB 1jaw: Aminopeptidase P From E. Coli Low pH Form

All present enzymatic activity of Aminopeptidase P From E. Coli Low pH Form:
3.4.11.9;

The structure of Aminopeptidase P From E. Coli Low pH Form, PDB code: 1jaw was solved by M.C.J.Wilce, C.S.Bond, P.E.Lilley, N.E.Dixon, 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)	50.00 / 2.70
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	139.710, 139.710, 230.870, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 22.7

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

Manganese binding site 1 out of 2 in the Aminopeptidase P From E. Coli Low pH Form


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Aminopeptidase P From E. Coli Low pH Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn441 b:30.6 occ:1.00 NE2 A:HIS354 2.0 28.0 1.0 OD2 A:ASP271 2.2 32.1 1.0 O A:ACT443 2.2 28.2 1.0 OE2 A:GLU406 2.3 19.2 1.0 OE2 A:GLU383 2.5 40.5 1.0 OE1 A:GLU406 2.9 14.1 1.0 MN A:MN442 2.9 29.5 1.0 CD A:GLU383 3.1 38.2 1.0 OE1 A:GLU383 3.1 38.1 1.0 CE1 A:HIS354 3.1 25.3 1.0 CD A:GLU406 3.1 18.1 1.0 CD2 A:HIS354 3.1 28.4 1.0 CG A:ASP271 3.2 31.9 1.0 C A:ACT443 3.2 26.2 1.0 OXT A:ACT443 3.5 30.4 1.0 OD1 A:ASP271 3.7 34.2 1.0 CG2 A:THR381 3.8 30.6 1.0 OG1 A:THR381 3.9 27.2 1.0 CB A:THR381 4.1 29.6 1.0 CB A:ASP271 4.1 29.4 1.0 ND1 A:HIS354 4.3 26.1 1.0 CG A:GLU383 4.3 32.2 1.0 CH3 A:ACT443 4.3 28.1 1.0 CG A:HIS354 4.3 28.4 1.0 CG A:GLU406 4.5 13.8 1.0 OD2 A:ASP260 4.8 24.4 1.0 NE2 A:HIS361 4.8 28.6 1.0 CB A:GLU383 4.9 29.2 1.0

Manganese binding site 2 out of 2 in the Aminopeptidase P From E. Coli Low pH Form


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Aminopeptidase P From E. Coli Low pH Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn442 b:29.5 occ:1.00 OE1 A:GLU406 1.8 14.1 1.0 OD2 A:ASP260 2.2 24.4 1.0 O A:ACT443 2.3 28.2 1.0 OD1 A:ASP260 2.3 28.9 1.0 OD1 A:ASP271 2.4 34.2 1.0 CG A:ASP260 2.6 25.7 1.0 C A:ACT443 2.8 26.2 1.0 CH3 A:ACT443 2.9 28.1 1.0 MN A:MN441 2.9 30.6 1.0 CG A:ASP271 3.1 31.9 1.0 CD A:GLU406 3.1 18.1 1.0 OD2 A:ASP271 3.2 32.1 1.0 OG1 A:THR273 3.5 24.9 1.0 OE2 A:GLU406 3.5 19.2 1.0 OH A:TYR229 3.8 24.2 1.0 OXT A:ACT443 3.9 30.4 1.0 OE1 A:GLU383 4.0 38.1 1.0 CB A:ASP260 4.1 24.0 1.0 CZ A:TYR229 4.2 20.7 1.0 CB A:ASP271 4.2 29.4 1.0 CG A:GLU406 4.2 13.8 1.0 CA A:ASP271 4.4 28.7 1.0 CE2 A:TYR229 4.6 23.0 1.0 C A:ASP271 4.6 28.1 1.0 CB A:GLU406 4.7 20.2 1.0 N A:ILE272 4.7 27.9 1.0 NE2 A:HIS354 4.8 28.0 1.0 CD A:GLU383 4.8 38.2 1.0 O A:ILE272 4.8 29.4 1.0 CE1 A:TYR229 4.8 20.4 1.0 NE A:ARG404 4.9 31.9 1.0 C A:ILE272 4.9 29.4 1.0 OE2 A:GLU383 4.9 40.5 1.0 CA A:ASP260 4.9 26.3 1.0 CB A:THR273 4.9 21.2 1.0

M.C.Wilce, C.S.Bond, N.E.Dixon, H.C.Freeman, J.M.Guss, P.E.Lilley, J.A.Wilce. Structure and Mechanism of A Proline-Specific Aminopeptidase From Escherichia Coli. Proc.Natl.Acad.Sci.Usa V. 95 3472 1998.
ISSN: ISSN 0027-8424
PubMed: 9520390
DOI: 10.1073/PNAS.95.7.3472