Zinc 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:

Manganese

(Mn)

2 atoms

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

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Perr-Zn-Mn within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn202 b:65.4 occ:1.00 SG A:CYS99 2.0 61.8 1.0 SG A:CYS96 2.2 59.1 1.0 SG A:CYS136 2.2 60.4 1.0 SG A:CYS139 2.3 65.4 1.0 CB A:CYS139 2.9 65.7 1.0 CB A:CYS99 3.2 61.8 1.0 CB A:CYS96 3.4 59.3 1.0 CB A:CYS136 3.6 61.8 1.0 N A:CYS99 3.6 61.3 1.0 CA A:CYS139 3.8 65.7 1.0 CA A:CYS99 3.9 61.9 1.0 N A:CYS136 4.1 61.7 1.0 N A:SER140 4.4 65.7 1.0 CA A:CYS136 4.5 62.1 1.0 CB A:ASN98 4.5 60.6 1.0 N A:GLY100 4.6 62.8 1.0 C A:CYS99 4.7 62.3 1.0 C A:ASN98 4.7 60.9 1.0 C A:CYS139 4.7 65.8 1.0 CA A:CYS96 4.7 59.4 1.0 N A:CYS139 4.8 65.5 1.0 ND2 A:ASN98 4.9 60.4 1.0 CA A:ASN98 5.0 60.5 1.0

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Perr-Zn-Mn within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn204 b:81.9 occ:1.00 SG B:CYS136 1.8 65.0 1.0 SG B:CYS96 2.4 67.2 1.0 SG B:CYS99 2.4 69.5 1.0 SG B:CYS139 2.5 73.5 1.0 CB B:CYS139 2.9 72.7 1.0 CB B:CYS96 3.2 67.3 1.0 CB B:CYS136 3.3 67.5 1.0 CB B:CYS99 3.3 71.3 1.0 N B:CYS99 3.7 70.9 1.0 CA B:CYS139 3.8 72.7 1.0 N B:CYS136 3.9 67.3 1.0 CA B:CYS99 4.0 71.3 1.0 CA B:CYS136 4.2 67.7 1.0 CD B:LYS101 4.2 73.5 1.0 C B:CYS139 4.5 72.7 1.0 CG B:LYS101 4.5 73.2 1.0 CB B:ASN98 4.6 70.2 1.0 N B:GLY100 4.7 72.3 1.0 CA B:CYS96 4.7 67.4 1.0 C B:CYS99 4.8 71.9 1.0 C B:ASN98 4.8 70.5 1.0 N B:CYS139 4.9 72.4 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