Mercury in PDB 1fe4: Crystal Structure of Mercury-HAH1

The structure of Crystal Structure of Mercury-HAH1, PDB code: 1fe4 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)	30.00 / 1.75
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	79.950, 79.950, 55.610, 90.00, 90.00, 120.00
R / Rfree (%)	20.4 / 21.8

The structure of Crystal Structure of Mercury-HAH1 also contains other interesting chemical elements:

Uranium

(U)

1 atom

The binding sites of Mercury atom in the Crystal Structure of Mercury-HAH1 (pdb code 1fe4). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Crystal Structure of Mercury-HAH1, PDB code: 1fe4:

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


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of Mercury-HAH1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg1007 b:27.2 occ:0.71 SG A:CYS12 2.3 28.9 1.0 SG B:CYS12 2.5 24.5 1.0 SG A:CYS15 2.5 24.7 1.0 SG B:CYS15 2.8 24.3 1.0 CB A:CYS12 3.3 28.5 1.0 CB B:CYS12 3.6 24.7 1.0 CB A:CYS15 3.8 24.6 1.0 N A:CYS15 3.8 21.0 1.0 N A:CYS12 3.9 21.1 1.0 N B:CYS15 3.9 22.1 1.0 CB B:CYS15 4.1 24.2 1.0 OG1 B:THR11 4.1 34.8 1.0 N B:CYS12 4.1 20.2 1.0 CA A:CYS12 4.1 21.2 1.0 OG1 A:THR11 4.1 24.5 1.0 CA A:CYS15 4.2 21.0 1.0 CA B:CYS12 4.4 20.0 1.0 CA B:CYS15 4.4 22.1 1.0 C A:THR11 4.4 25.1 1.0 O A:HOH1040 4.5 28.0 1.0 C A:CYS12 4.6 21.1 1.0 C A:GLY14 4.6 22.6 1.0 O A:CYS12 4.6 21.1 1.0 C B:GLY14 4.7 22.9 1.0 C B:CYS12 4.8 19.8 1.0 O B:CYS12 4.8 19.9 1.0 N A:THR11 4.8 25.0 1.0 CA A:GLY14 4.8 22.7 1.0 C B:THR11 4.9 28.8 1.0 CA B:GLY14 4.9 23.0 1.0 N A:GLY14 4.9 22.7 1.0 CA A:THR11 4.9 25.1 1.0 O A:THR11 4.9 25.2 1.0 N B:GLY14 5.0 22.9 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