Mercury in PDB 2a1i: Crystal Structure of the Central Domain of Human ERCC1

The structure of Crystal Structure of the Central Domain of Human ERCC1, PDB code: 2a1i was solved by O.V.Tsodikov, J.H.Enzlin, O.D.Scharer, T.Ellenberger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.070, 50.291, 72.216, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 24.8

The binding sites of Mercury atom in the Crystal Structure of the Central Domain of Human ERCC1 (pdb code 2a1i). 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 the Central Domain of Human ERCC1, PDB code: 2a1i:

Mercury binding site 1 out of 1 in the Crystal Structure of the Central Domain of Human ERCC1


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 the Central Domain of Human ERCC1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg1 b:76.3 occ:0.60 SG A:CYS137 2.7 29.7 1.0 CD2 A:LEU160 2.8 41.4 1.0 O A:CYS137 3.2 23.7 1.0 CB A:ARG167 3.4 29.1 1.0 C A:CYS137 3.5 25.3 1.0 CA A:ARG167 3.6 29.7 1.0 N A:ALA138 3.8 24.3 1.0 N A:VAL168 3.8 28.6 1.0 CG A:ARG167 3.8 31.9 1.0 CA A:ALA138 3.9 24.2 1.0 CB A:CYS137 3.9 26.7 1.0 C A:ALA138 4.0 23.5 1.0 CG A:LEU160 4.1 42.6 1.0 N A:LEU139 4.1 23.4 1.0 O A:VAL168 4.1 26.8 1.0 C A:ARG167 4.2 29.6 1.0 CD2 A:LEU139 4.2 30.1 1.0 CD1 A:LEU160 4.3 42.4 1.0 CA A:CYS137 4.3 26.1 1.0 O A:ALA138 4.5 23.2 1.0 CB A:PRO128 4.6 24.4 1.0 C A:VAL168 4.7 27.2 1.0 CG A:LEU139 4.8 28.0 1.0 N A:CYS137 4.8 26.4 1.0 CA A:VAL168 4.9 28.1 1.0 CD1 A:LEU139 5.0 24.9 1.0 N A:ARG167 5.0 29.0 1.0

O.V.Tsodikov, J.H.Enzlin, O.D.Scharer, T.Ellenberger. Crystal Structure and Dna Binding Functions of ERCC1, A Subunit of the Dna Structure-Specific Endonuclease Xpf-ERCC1. Proc.Natl.Acad.Sci.Usa V. 102 11236 2005.
ISSN: ISSN 0027-8424
PubMed: 16076955
DOI: 10.1073/PNAS.0504341102