Manganese in PDB 2bws: HIS243ALA Escherichia Coli Aminopeptidase P

All present enzymatic activity of HIS243ALA Escherichia Coli Aminopeptidase P:
3.4.11.9;

The structure of HIS243ALA Escherichia Coli Aminopeptidase P, PDB code: 2bws was solved by S.C.Graham, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.08 / 1.75
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	177.147, 177.147, 96.438, 90.00, 90.00, 120.00
R / Rfree (%)	15 / 16.5

The structure of HIS243ALA Escherichia Coli Aminopeptidase P also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Manganese atom in the HIS243ALA Escherichia Coli Aminopeptidase P (pdb code 2bws). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the HIS243ALA Escherichia Coli Aminopeptidase P, PDB code: 2bws:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the HIS243ALA Escherichia Coli Aminopeptidase P


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of HIS243ALA Escherichia Coli Aminopeptidase P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1441 b:19.2 occ:1.00 O A:HOH2641 1.9 21.1 1.0 OE2 A:GLU406 2.0 25.6 1.0 NE2 A:HIS354 2.1 22.6 1.0 OD2 A:ASP271 2.2 26.6 1.0 OE2 A:GLU383 2.3 32.9 1.0 CD A:GLU383 3.0 31.1 1.0 CD A:GLU406 3.0 26.5 1.0 MN A:MN1442 3.1 17.4 0.8 CG A:ASP271 3.1 25.4 1.0 CE1 A:HIS354 3.1 26.2 1.0 CD2 A:HIS354 3.1 24.6 1.0 OE1 A:GLU383 3.1 36.1 1.0 OD1 A:ASP271 3.3 25.2 1.0 OE1 A:GLU406 3.4 26.1 1.0 O A:HOH2544 3.4 34.4 1.0 CG2 A:THR381 3.7 26.5 1.0 OG1 A:THR381 3.8 22.6 1.0 O A:HOH2642 3.9 31.6 1.0 CB A:THR381 4.0 24.6 1.0 ND1 A:HIS354 4.2 21.9 1.0 CG A:HIS354 4.2 21.2 1.0 CG A:GLU406 4.4 24.2 1.0 CB A:ASP271 4.4 22.5 1.0 CG A:GLU383 4.4 26.3 1.0 CB A:GLU383 4.9 27.4 1.0 NE2 A:HIS361 4.9 29.6 1.0 CG2 A:VAL360 4.9 25.3 1.0

Manganese binding site 2 out of 2 in the HIS243ALA Escherichia Coli Aminopeptidase P


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of HIS243ALA Escherichia Coli Aminopeptidase P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1442 b:17.4 occ:0.80 O A:HOH2641 2.0 21.1 1.0 OD1 A:ASP271 2.0 25.2 1.0 OE1 A:GLU406 2.1 26.1 1.0 OD1 A:ASP260 2.2 26.5 1.0 O A:HOH2642 2.4 31.6 1.0 OD2 A:ASP260 2.5 26.7 1.0 CG A:ASP260 2.6 27.9 1.0 CD A:GLU406 3.0 26.5 1.0 CG A:ASP271 3.0 25.4 1.0 MN A:MN1441 3.1 19.2 1.0 OE2 A:GLU406 3.2 25.6 1.0 OD2 A:ASP271 3.2 26.6 1.0 OG1 A:THR273 3.5 22.7 1.0 OH A:TYR229 3.8 24.7 1.0 OE1 A:GLU383 3.9 36.1 1.0 O A:HOH2544 4.1 34.4 1.0 CB A:ASP260 4.2 23.4 1.0 CZ A:TYR229 4.3 24.8 1.0 O A:HOH2452 4.4 50.8 1.0 CG A:GLU406 4.4 24.2 1.0 CB A:ASP271 4.4 22.5 1.0 C A:ASP271 4.6 25.3 1.0 O A:ILE272 4.6 22.4 1.0 CD A:GLU383 4.6 31.1 1.0 CE2 A:TYR229 4.7 25.7 1.0 OE2 A:GLU383 4.7 32.9 1.0 C A:ILE272 4.7 22.7 1.0 N A:ILE272 4.8 22.9 1.0 CA A:ASP271 4.8 22.5 1.0 NE A:ARG404 4.8 24.5 1.0 O A:ASP271 4.8 23.9 1.0 CA A:ASP260 4.9 22.8 1.0 CB A:THR273 4.9 23.1 1.0 N A:THR273 4.9 22.1 1.0 CB A:GLU406 4.9 23.8 1.0 O A:HOH2546 4.9 46.0 1.0

S.C.Graham, P.E.Lilley, M.Lee, P.M.Schaeffer, A.V.Kralicek, N.E.Dixon, J.M.Guss. Kinetic and Crystallographic Analysis of Mutant Escherichia Coli Aminopeptidase P: Insights Into Substrate Recognition and the Mechanism of Catalysis. Biochemistry V. 45 964 2006.
ISSN: ISSN 0006-2960
PubMed: 16411772
DOI: 10.1021/BI0518904