Mercury in PDB 2h94: Crystal Structure and Mechanism of Human Lysine-Specific Demethylase-1

The structure of Crystal Structure and Mechanism of Human Lysine-Specific Demethylase-1, PDB code: 2h94 was solved by P.Stavropoulos, G.Blobel, A.Hoelz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.90
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	187.943, 187.943, 108.741, 90.00, 90.00, 120.00
R / Rfree (%)	22.9 / 28.1

The binding sites of Mercury atom in the Crystal Structure and Mechanism of Human Lysine-Specific Demethylase-1 (pdb code 2h94). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Crystal Structure and Mechanism of Human Lysine-Specific Demethylase-1, PDB code: 2h94:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in the Crystal Structure and Mechanism of Human Lysine-Specific Demethylase-1


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure and Mechanism of Human Lysine-Specific Demethylase-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg1 b:0.9 occ:1.00 SG A:CYS360 2.7 80.5 1.0 CB A:CYS360 3.0 80.5 1.0 O A:CYS360 3.3 81.2 1.0 CD2 A:LEU362 3.3 80.5 1.0 C A:CYS360 3.5 79.4 1.0 CH2 A:TRP531 3.6 43.1 1.0 CG A:LEU362 3.8 79.6 1.0 CA A:CYS360 3.9 79.9 1.0 CZ2 A:TRP531 3.9 45.9 1.0 CZ3 A:TRP531 4.2 45.8 1.0 N A:PRO361 4.2 77.4 1.0 O A:PRO361 4.4 75.9 1.0 C A:PRO361 4.4 76.2 1.0 N A:GLY679 4.5 66.1 1.0 CD1 A:LEU362 4.6 80.2 1.0 N A:LEU362 4.7 76.3 1.0 CA A:PRO361 4.7 76.3 1.0 CE2 A:TRP531 4.7 48.7 1.0 N A:CYS360 4.9 80.4 1.0 CB A:LEU362 4.9 77.9 1.0 CE3 A:TRP531 5.0 46.1 1.0

Mercury binding site 2 out of 3 in the Crystal Structure and Mechanism of Human Lysine-Specific Demethylase-1


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystal Structure and Mechanism of Human Lysine-Specific Demethylase-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg2 b:0.7 occ:1.00 OE1 A:GLN419 3.6 85.0 1.0 CD A:GLN419 4.1 83.3 1.0 CB A:ALA388 4.1 52.5 1.0 NE2 A:GLN419 4.2 84.6 1.0 CG1 A:VAL415 4.6 65.7 1.0

Mercury binding site 3 out of 3 in the Crystal Structure and Mechanism of Human Lysine-Specific Demethylase-1


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Crystal Structure and Mechanism of Human Lysine-Specific Demethylase-1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg3 b:0.4 occ:1.00 CB A:CYS573 3.3 79.3 1.0 SG A:CYS573 3.3 92.2 1.0 CA A:CYS573 3.7 74.2 1.0 CG1 A:VAL349 4.2 67.5 1.0 O A:CYS573 4.4 69.7 1.0 C A:CYS573 4.4 70.8 1.0 ND2 A:ASN569 4.7 84.2 1.0 O A:VAL349 4.7 68.8 1.0 N A:CYS573 4.9 73.4 1.0

P.Stavropoulos, G.Blobel, A.Hoelz. Crystal Structure and Mechanism of Human Lysine-Specific Demethylase-1. Nat.Struct.Mol.Biol. V. 13 626 2006.
ISSN: ISSN 1545-9993
PubMed: 16799558
DOI: 10.1038/NSMB1113