Manganese in PDB 3f8n: Crystal Structure of Perr-Zn-Mn

The structure of Crystal Structure of Perr-Zn-Mn, PDB code: 3f8n was solved by D.A.K.Traore, J.-L.Ferrer, L.Jacquamet, V.Duarte, J.-M.Latour, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.64 / 3.15
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.300, 63.340, 66.730, 90.00, 80.41, 90.00
R / Rfree (%)	27.5 / 31.5

The structure of Crystal Structure of Perr-Zn-Mn also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Manganese atom in the Crystal Structure of Perr-Zn-Mn (pdb code 3f8n). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Perr-Zn-Mn, PDB code: 3f8n:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Perr-Zn-Mn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Perr-Zn-Mn within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:70.6 occ:1.00 NE2 A:HIS91 2.1 74.2 1.0 NE2 A:HIS93 2.2 64.6 1.0 OD2 A:ASP104 2.4 70.0 1.0 OD2 A:ASP85 2.4 78.6 1.0 NE2 A:HIS37 2.5 71.2 1.0 OD1 A:ASP104 2.7 68.4 1.0 CD2 A:HIS91 2.9 74.5 1.0 CG A:ASP104 2.9 68.9 1.0 CE1 A:HIS93 3.0 65.0 1.0 O A:HOH301 3.1 64.3 1.0 CD2 A:HIS93 3.1 64.7 1.0 CE1 A:HIS91 3.2 74.2 1.0 CD2 A:HIS37 3.2 71.3 1.0 CG A:ASP85 3.2 79.2 1.0 CE1 A:HIS37 3.5 70.7 1.0 OD1 A:ASP85 3.8 77.6 1.0 ND1 A:HIS93 4.1 65.0 1.0 CG A:HIS91 4.1 73.9 1.0 CG A:HIS93 4.2 65.0 1.0 ND1 A:HIS91 4.2 74.3 1.0 CB A:ASP85 4.2 80.3 1.0 CB A:ASP104 4.4 68.5 1.0 CG A:HIS37 4.4 71.8 1.0 ND1 A:HIS37 4.6 70.3 1.0 O A:TYR92 5.0 67.2 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Perr-Zn-Mn


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Perr-Zn-Mn within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn203 b:59.0 occ:1.00 NE2 B:HIS91 2.0 73.3 1.0 NE2 B:HIS93 2.1 62.2 1.0 OD1 B:ASP85 2.2 78.6 1.0 NE2 B:HIS37 2.2 63.3 1.0 OD2 B:ASP104 2.3 72.8 1.0 CE1 B:HIS91 2.9 73.5 1.0 CD2 B:HIS93 3.0 63.4 1.0 CG B:ASP85 3.0 79.0 1.0 CD2 B:HIS91 3.0 72.7 1.0 CE1 B:HIS37 3.1 63.3 1.0 OD2 B:ASP85 3.1 78.0 1.0 CE1 B:HIS93 3.2 62.4 1.0 CD2 B:HIS37 3.3 63.5 1.0 CG B:ASP104 3.3 72.8 1.0 OD1 B:ASP104 3.7 72.5 1.0 ND1 B:HIS91 4.0 72.6 1.0 CG B:HIS91 4.1 71.9 1.0 CG B:HIS93 4.2 64.8 1.0 ND1 B:HIS93 4.2 62.8 1.0 ND1 B:HIS37 4.2 63.3 1.0 CG B:HIS37 4.3 63.9 1.0 CB B:ASP85 4.4 79.5 1.0 CB B:ASP104 4.6 72.4 1.0 CA B:ASP104 4.8 72.3 1.0 O B:ILE102 4.9 74.6 1.0

L.Jacquamet, D.A.K.Traore, J.-L.Ferrer, O.Proux, D.Testemale, J.-L.Hazemann, E.Nazarenko, A.El Ghazouani, C.Caux-Thang, V.Duarte, J.-M.Latour. Structural Characterization of the Active Form of Perr: Insights Into the Metal-Induced Activation of Perr and Fur Proteins For Dna Binding Mol.Microbiol. V. 73 20 2009.
ISSN: ISSN 0950-382X
PubMed: 19508285
DOI: 10.1111/J.1365-2958.2009.06753.X