Copper in PDB 1fee: Crystal Structure of Copper-HAH1

The structure of Crystal Structure of Copper-HAH1, PDB code: 1fee was solved by A.K.Wernimont, D.L.Huffman, A.L.Lamb, T.V.O'halloran, A.C.Rosenzweig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.80
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	78.232, 78.232, 54.664, 90.00, 90.00, 120.00
R / Rfree (%)	19.1 / 21.6

The binding sites of Copper atom in the Crystal Structure of Copper-HAH1 (pdb code 1fee). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of Copper-HAH1, PDB code: 1fee:

Copper binding site 1 out of 1 in the Crystal Structure of Copper-HAH1


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Copper-HAH1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu173 b:19.5 occ:0.90 SG A:CYS12 2.3 21.0 1.0 SG B:CYS12 2.3 19.3 1.0 SG B:CYS15 2.3 20.5 1.0 SG A:CYS15 2.4 18.6 1.0 CB B:CYS12 3.3 19.7 1.0 CB A:CYS12 3.4 17.9 1.0 CB A:CYS15 3.6 17.8 1.0 CB B:CYS15 3.6 19.0 1.0 N B:CYS15 3.7 18.5 1.0 N A:CYS15 3.7 17.4 1.0 N B:CYS12 3.9 19.8 1.0 N A:CYS12 3.9 20.6 1.0 CA A:CYS15 4.0 17.4 1.0 CA B:CYS12 4.1 19.2 1.0 CA B:CYS15 4.1 18.2 1.0 CA A:CYS12 4.2 20.3 1.0 OG1 A:THR11 4.2 22.5 1.0 OG1 B:THR11 4.3 27.4 1.0 O A:HOH237 4.4 31.6 1.0 C A:THR11 4.5 23.4 1.0 O B:CYS12 4.5 17.7 1.0 C B:CYS12 4.5 18.2 1.0 C B:THR11 4.5 26.4 1.0 C B:GLY14 4.6 18.0 1.0 O A:CYS12 4.6 19.1 1.0 C A:GLY14 4.6 17.8 1.0 C A:CYS12 4.6 20.1 1.0 N A:THR11 4.7 21.4 1.0 N B:THR11 4.8 24.4 1.0 CA B:GLY14 4.9 18.0 1.0 N B:GLY14 4.9 18.2 1.0 CA A:GLY14 4.9 17.8 1.0 CA A:THR11 5.0 22.6 1.0 N A:GLY14 5.0 17.8 1.0 O A:THR11 5.0 25.4 1.0

A.K.Wernimont, D.L.Huffman, A.L.Lamb, T.V.O'halloran, A.C.Rosenzweig. Structural Basis For Copper Transfer By the Metallochaperone For the Menkes/Wilson Disease Proteins. Nat.Struct.Biol. V. 7 766 2000.
ISSN: ISSN 1072-8368
PubMed: 10966647
DOI: 10.1038/78999