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Mercury in PDB 2v66: Crystal Structure of the Coiled-Coil Domain of NDEL1 (A.A. 58 to 169)C

Protein crystallography data

The structure of Crystal Structure of the Coiled-Coil Domain of NDEL1 (A.A. 58 to 169)C, PDB code: 2v66 was solved by C.Tarricone, F.Perrina, A.Musacchio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.00 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 46.431, 73.221, 69.026, 90.00, 105.40, 90.00
R / Rfree (%) 23.3 / 31

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of the Coiled-Coil Domain of NDEL1 (A.A. 58 to 169)C (pdb code 2v66). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Crystal Structure of the Coiled-Coil Domain of NDEL1 (A.A. 58 to 169)C, PDB code: 2v66:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in 2v66

Go back to Mercury Binding Sites List in 2v66
Mercury binding site 1 out of 2 in the Crystal Structure of the Coiled-Coil Domain of NDEL1 (A.A. 58 to 169)C


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 Coiled-Coil Domain of NDEL1 (A.A. 58 to 169)C within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg1169

b:40.9
occ:0.50
O B:GLU98 3.3 26.2 1.0
OG B:SER102 3.8 21.5 1.0
C B:GLU98 4.0 25.8 1.0
CB B:GLU98 4.1 27.2 1.0
CA B:GLU98 4.2 27.4 1.0
N B:SER102 4.2 18.4 1.0
CB B:LEU101 4.2 24.2 1.0
CB B:SER102 4.5 17.8 1.0
CG B:GLU98 4.5 27.6 1.0
CA B:SER102 4.7 18.9 1.0

Mercury binding site 2 out of 2 in 2v66

Go back to Mercury Binding Sites List in 2v66
Mercury binding site 2 out of 2 in the Crystal Structure of the Coiled-Coil Domain of NDEL1 (A.A. 58 to 169)C


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystal Structure of the Coiled-Coil Domain of NDEL1 (A.A. 58 to 169)C within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Hg1169

b:51.7
occ:0.33
CB E:SER102 2.9 26.9 1.0
CA E:SER102 3.5 26.2 1.0
O E:SER102 4.1 24.5 1.0
C E:SER102 4.3 26.4 1.0
OG E:SER102 4.3 35.8 1.0
N E:SER102 4.7 25.5 1.0
CD E:ARG105 4.8 24.6 1.0

Reference:

U.Derewenda, C.Tarricone, W.C.Choi, D.R.Cooper, S.Lukasik, F.Perrina, A.Tripathy, M.H.Kim, D.S.Cafiso, A.Musacchio, Z.S.Derewenda. The Structure of the Coiled-Coil Domain of NDEL1 and the Basis of Its Interaction with LIS1, the Causal Protein of Miller-Dieker Lissencephaly. Structure V. 15 1467 2007.
ISSN: ISSN 0969-2126
PubMed: 17997972
DOI: 10.1016/J.STR.2007.09.015
Page generated: Wed Oct 28 18:41:59 2020

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