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Mercury in PDB 1t3s: Structural Analysis of the Voltage-Dependent Calcium Channel Beta Subunit Functional Core

Protein crystallography data

The structure of Structural Analysis of the Voltage-Dependent Calcium Channel Beta Subunit Functional Core, PDB code: 1t3s was solved by Y.Opatowsky, C.-C.Chen, K.P.Campbell, J.A.Hirsch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 81.65 / 2.30
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 74.066, 163.841, 34.761, 90.00, 90.00, 90.00
R / Rfree (%) 26.1 / 27.7

Mercury Binding Sites:

The binding sites of Mercury atom in the Structural Analysis of the Voltage-Dependent Calcium Channel Beta Subunit Functional Core (pdb code 1t3s). 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 Structural Analysis of the Voltage-Dependent Calcium Channel Beta Subunit Functional Core, PDB code: 1t3s:

Mercury binding site 1 out of 1 in 1t3s

Go back to Mercury Binding Sites List in 1t3s
Mercury binding site 1 out of 1 in the Structural Analysis of the Voltage-Dependent Calcium Channel Beta Subunit Functional Core


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structural Analysis of the Voltage-Dependent Calcium Channel Beta Subunit Functional Core within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1

b:88.7
occ:1.00
SG A:CYS114 2.7 76.2 1.0
CB A:CYS114 3.6 67.0 1.0
O A:GLU115 3.7 69.3 1.0
CD1 A:ILE86 3.8 59.7 1.0
CG1 A:ILE86 3.8 58.1 1.0
CG2 A:ILE86 4.1 57.6 1.0
CA A:CYS114 4.1 65.6 1.0
N A:GLU115 4.3 67.3 1.0
C A:CYS114 4.5 66.3 1.0
CB A:LEU109 4.5 52.3 1.0
CB A:ILE86 4.5 56.3 1.0
N A:LEU109 4.7 50.5 1.0
C A:GLU115 4.8 67.0 1.0
CD1 A:LEU109 4.8 55.6 1.0

Reference:

Y.Opatowsky, C.C.Chen, K.P.Campbell, J.A.Hirsch. Structural Analysis of the Voltage-Dependent Calcium Channel Beta Subunit Functional Core and Its Complex with the Alpha 1 Interaction Domain. Neuron V. 42 387 2004.
ISSN: ISSN 0896-6273
PubMed: 15134636
DOI: 10.1093/HMG/DDH162
Page generated: Sun Dec 13 19:05:19 2020

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