Manganese in PDB 2bww: HIS350ALA Escherichia Coli Aminopeptidase P

All present enzymatic activity of HIS350ALA Escherichia Coli Aminopeptidase P:
3.4.11.9;

The structure of HIS350ALA Escherichia Coli Aminopeptidase P, PDB code: 2bww 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)	69.67 / 2.61
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	138.170, 138.170, 231.296, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 20.4

The structure of HIS350ALA Escherichia Coli Aminopeptidase P also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Manganese atom in the HIS350ALA Escherichia Coli Aminopeptidase P (pdb code 2bww). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the HIS350ALA Escherichia Coli Aminopeptidase P, PDB code: 2bww:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the HIS350ALA 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 HIS350ALA Escherichia Coli Aminopeptidase P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1441 b:42.3 occ:1.00 O A:HOH2151 2.0 35.2 1.0 OE2 A:GLU406 2.1 40.7 1.0 NE2 A:HIS354 2.1 46.5 1.0 OD2 A:ASP271 2.2 44.8 1.0 OE2 A:GLU383 2.4 46.6 1.0 O A:HOH2115 3.1 38.3 1.0 CE1 A:HIS354 3.1 46.5 1.0 CD A:GLU406 3.1 43.8 1.0 CD A:GLU383 3.1 48.0 1.0 CD2 A:HIS354 3.1 45.4 1.0 CG A:ASP271 3.2 46.8 1.0 OE1 A:GLU383 3.2 47.7 1.0 MN A:MN1442 3.2 39.2 1.0 OE1 A:GLU406 3.4 43.2 1.0 OD1 A:ASP271 3.6 47.6 1.0 CG2 A:THR381 3.8 45.2 1.0 OG1 A:THR381 3.8 42.9 1.0 O A:HOH2152 3.9 36.0 1.0 CB A:THR381 4.1 44.4 1.0 ND1 A:HIS354 4.2 45.5 1.0 CG A:HIS354 4.2 45.3 1.0 CB A:ASP271 4.4 47.1 1.0 CG A:GLU406 4.4 44.6 1.0 CG A:GLU383 4.5 47.2 1.0 O2 A:MRD1445 4.6 75.0 1.0 NE2 A:HIS361 4.7 46.7 1.0 CD2 A:HIS361 4.9 45.6 1.0 CG2 A:VAL360 5.0 46.2 1.0

Manganese binding site 2 out of 2 in the HIS350ALA 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 HIS350ALA Escherichia Coli Aminopeptidase P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1442 b:39.2 occ:1.00 OD1 A:ASP271 2.1 47.6 1.0 OE1 A:GLU406 2.2 43.2 1.0 OD2 A:ASP260 2.3 48.4 1.0 O A:HOH2152 2.3 36.0 1.0 OD1 A:ASP260 2.4 41.9 1.0 O A:HOH2151 2.4 35.2 1.0 CG A:ASP260 2.7 44.4 1.0 CG A:ASP271 3.0 46.8 1.0 CD A:GLU406 3.0 43.8 1.0 OD2 A:ASP271 3.2 44.8 1.0 MN A:MN1441 3.2 42.3 1.0 OE2 A:GLU406 3.3 40.7 1.0 OG1 A:THR273 3.7 46.6 1.0 O A:HOH2115 3.7 38.3 1.0 OH A:TYR229 3.8 45.5 1.0 CZ A:TYR229 4.2 45.2 1.0 CB A:ASP260 4.2 45.8 1.0 OE1 A:GLU383 4.3 47.7 1.0 CG A:GLU406 4.4 44.6 1.0 CB A:ASP271 4.4 47.1 1.0 CE2 A:TYR229 4.5 45.1 1.0 O A:ILE272 4.7 45.2 1.0 O2 A:MRD1445 4.7 75.0 1.0 C A:ASP271 4.7 45.9 1.0 NE A:ARG404 4.8 47.0 1.0 CE1 A:TYR229 4.8 43.6 1.0 CA A:ASP271 4.9 46.6 1.0 C A:ILE272 4.9 46.1 1.0 N A:ILE272 4.9 46.3 1.0 CB A:GLU406 4.9 45.2 1.0 O A:ASP271 5.0 45.5 1.0 NH2 A:ARG404 5.0 48.1 1.0 CD A:GLU383 5.0 48.0 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