Copper in PDB 8t7l: Copper Bound Hfta From Treponema Denticola

The structure of Copper Bound Hfta From Treponema Denticola, PDB code: 8t7l was solved by B.W.Corbett, M.D.Suits, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.17 / 1.89
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	31.51, 78.16, 150.27, 90, 90, 90
R / Rfree (%)	20.8 / 23.3

The binding sites of Copper atom in the Copper Bound Hfta From Treponema Denticola (pdb code 8t7l). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Copper Bound Hfta From Treponema Denticola, PDB code: 8t7l:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Copper Bound Hfta From Treponema Denticola


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Copper Bound Hfta From Treponema Denticola within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu302 b:28.7 occ:1.00 NE2 A:HIS94 2.0 26.4 1.0 NE2 A:HIS148 2.0 28.4 1.0 NE2 B:HIS178 2.1 27.0 1.0 SD A:MET141 2.4 31.5 1.0 CE1 A:HIS94 2.9 28.0 1.0 CE1 B:HIS178 2.9 31.6 1.0 CD2 A:HIS148 3.0 25.6 1.0 CE1 A:HIS148 3.1 32.7 1.0 CD2 A:HIS94 3.1 28.0 1.0 CG A:MET141 3.2 29.0 1.0 CD2 B:HIS178 3.2 28.4 1.0 CE A:MET141 3.5 27.1 1.0 ND1 A:HIS94 4.0 27.2 1.0 ND1 B:HIS178 4.1 31.0 1.0 ND1 A:HIS148 4.1 32.5 1.0 CG A:HIS94 4.2 26.2 1.0 CG A:HIS148 4.2 28.8 1.0 CG B:HIS178 4.3 31.4 1.0 CA A:GLY150 4.3 24.8 1.0 CB A:MET141 4.5 28.8 1.0 N A:GLY150 4.7 23.9 1.0 C A:GLY150 4.8 28.9 1.0 OE2 A:GLU96 4.8 43.0 1.0 CG2 A:VAL77 4.9 29.2 1.0

Copper binding site 2 out of 2 in the Copper Bound Hfta From Treponema Denticola


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Copper Bound Hfta From Treponema Denticola within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu301 b:29.0 occ:1.00 NE2 B:HIS94 2.1 25.5 1.0 NE2 A:HIS178 2.1 27.9 1.0 NE2 B:HIS148 2.1 31.9 1.0 SD B:MET141 2.3 32.3 1.0 CE1 B:HIS94 2.9 27.3 1.0 CE1 A:HIS178 3.0 30.3 1.0 CE1 B:HIS148 3.1 33.6 1.0 CD2 B:HIS148 3.1 31.9 1.0 CG B:MET141 3.1 28.0 1.0 CD2 B:HIS94 3.1 29.5 1.0 CD2 A:HIS178 3.2 29.4 1.0 CE B:MET141 3.4 27.1 1.0 ND1 B:HIS94 4.0 28.2 1.0 ND1 A:HIS178 4.2 29.0 1.0 CG B:HIS94 4.2 24.8 1.0 CA B:GLY150 4.2 27.7 1.0 ND1 B:HIS148 4.2 36.5 1.0 CG B:HIS148 4.3 32.6 1.0 CG A:HIS178 4.3 29.8 1.0 CB B:MET141 4.5 28.5 1.0 OE1 B:GLU96 4.5 51.4 1.0 C B:GLY150 4.7 27.2 1.0 N B:GLY150 4.7 24.4 1.0 N B:ALA151 4.9 26.6 1.0 CG2 B:VAL77 4.9 30.2 1.0 SD B:MET79 5.0 39.8 1.0

B.W.Corbett, M.D.Suits. Structural and Functional Characterization of the High-Affinity Ferrous Iron Transport Protein Hfta From Treponema Denticola To Be Published.