Manganese in PDB 3n9d: Monoclinic Structure of P. Aeruginosa Ligd Phosphoesterase Domain

The structure of Monoclinic Structure of P. Aeruginosa Ligd Phosphoesterase Domain, PDB code: 3n9d was solved by S.Shuman, P.Nair, P.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.29 / 2.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.997, 56.585, 43.503, 90.00, 118.33, 90.00
R / Rfree (%)	21.2 / 26.3

The structure of Monoclinic Structure of P. Aeruginosa Ligd Phosphoesterase Domain also contains other interesting chemical elements:

Yttrium

(Y)

2 atoms

The binding sites of Manganese atom in the Monoclinic Structure of P. Aeruginosa Ligd Phosphoesterase Domain (pdb code 3n9d). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Monoclinic Structure of P. Aeruginosa Ligd Phosphoesterase Domain, PDB code: 3n9d:

Manganese binding site 1 out of 1 in the Monoclinic Structure of P. Aeruginosa Ligd Phosphoesterase Domain


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Monoclinic Structure of P. Aeruginosa Ligd Phosphoesterase Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1 b:30.8 occ:1.00 O3 A:SO4188 2.3 24.8 1.0 NE2 A:HIS48 2.3 24.1 1.0 OD2 A:ASP50 2.5 20.8 1.0 ND1 A:HIS42 2.6 26.1 1.0 CE1 A:HIS48 3.1 26.8 1.0 CG A:ASP50 3.4 25.2 1.0 S A:SO4188 3.4 33.0 1.0 CE1 A:HIS42 3.5 30.5 1.0 O1 A:SO4188 3.5 22.5 1.0 CD2 A:HIS48 3.5 24.9 1.0 OD1 A:ASP50 3.5 23.7 1.0 CG A:HIS42 3.5 28.2 1.0 CB A:HIS42 3.8 30.2 1.0 O A:HOH203 3.9 23.1 1.0 O4 A:SO4188 4.3 26.3 1.0 ND1 A:HIS48 4.3 27.9 1.0 O2 A:SO4188 4.3 35.0 1.0 O A:HOH204 4.4 24.5 1.0 CG A:HIS48 4.5 29.0 1.0 NE2 A:HIS42 4.6 33.8 1.0 CD2 A:HIS42 4.6 27.6 1.0 CB A:ASP50 4.8 29.2 1.0

P.A.Nair, P.Smith, S.Shuman. Structure of Bacterial Ligd 3'-Phosphoesterase Unveils A Dna Repair Superfamily Proc.Natl.Acad.Sci.Usa V. 107 12822 2010.
ISSN: ISSN 0027-8424
PubMed: 20616014
DOI: 10.1073/PNAS.1005830107