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Mercury in PDB 5c17: Crystal Structure of the Mercury-Bound Form of MERB2

Protein crystallography data

The structure of Crystal Structure of the Mercury-Bound Form of MERB2, PDB code: 5c17 was solved by H.M.Wahba, L.Lecoq, M.Stevenson, A.Mansour, L.Cappadocia, J.Lafrance-Vanasse, K.J.Wilkinson, J.Sygusch, D.E.Wilcox, J.G.Omichinski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.46 / 1.24
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 83.290, 53.421, 47.719, 90.00, 96.85, 90.00
R / Rfree (%) 14.2 / 16.1

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of the Mercury-Bound Form of MERB2 (pdb code 5c17). 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 Mercury-Bound Form of MERB2, PDB code: 5c17:

Mercury binding site 1 out of 1 in 5c17

Go back to Mercury Binding Sites List in 5c17
Mercury binding site 1 out of 1 in the Crystal Structure of the Mercury-Bound Form of MERB2


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 Mercury-Bound Form of MERB2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg301

b:16.7
occ:0.78
SG A:CYS102 2.4 11.7 1.0
SG A:CYS165 2.4 16.3 1.0
O A:HOH569 2.5 25.1 1.0
S4 A:DTV303 2.6 22.6 0.8
HG A:SER105 2.7 15.6 0.7
H4 A:DTV303 3.0 27.1 0.8
H4C1 A:DTV303 3.2 27.1 0.8
HB3 A:CYS102 3.2 10.8 1.0
OG A:SER105 3.3 13.0 0.7
HA A:CYS165 3.3 15.3 1.0
H3 A:DTV303 3.4 27.1 0.8
C4 A:DTV303 3.4 22.6 0.8
CB A:CYS102 3.4 9.0 1.0
HB3 A:CYS165 3.5 17.2 1.0
CB A:CYS165 3.5 14.3 1.0
HD12 A:ILE168 3.5 16.9 1.0
HG A:SER105 3.6 13.5 0.3
HB2 A:TRP101 3.8 11.1 1.0
HB3 A:SER105 3.8 12.4 0.3
C3 A:DTV303 3.9 22.6 0.8
CA A:CYS165 3.9 12.8 1.0
HD13 A:ILE168 4.0 16.9 1.0
HB2 A:CYS102 4.1 10.8 1.0
H A:SER105 4.1 10.9 0.7
H A:SER105 4.1 10.9 0.3
OG A:SER105 4.1 11.3 0.3
CD1 A:ILE168 4.2 14.1 1.0
H4C2 A:DTV303 4.3 27.1 0.8
HB A:ILE104 4.3 12.5 1.0
HB2 A:CYS165 4.3 17.2 1.0
N A:CYS102 4.3 8.8 1.0
O2 A:DTV303 4.3 22.7 0.8
H A:CYS102 4.4 10.6 1.0
HB3 A:TRP101 4.4 11.1 1.0
HE3 A:TRP101 4.4 11.4 1.0
CA A:CYS102 4.5 8.3 1.0
CB A:SER105 4.5 10.3 0.3
CB A:SER105 4.5 10.8 0.7
CB A:TRP101 4.5 9.2 1.0
HB2 A:SER105 4.6 13.0 0.7
HD11 A:ILE168 4.6 16.9 1.0
C A:TRP101 4.7 8.9 1.0
N A:CYS165 4.7 12.2 1.0
HA2 A:GLY81 4.8 10.4 1.0
HB A:ILE168 4.8 13.7 1.0
N A:SER105 4.8 9.1 1.0
C2 A:DTV303 4.8 21.8 0.8
H A:CYS165 4.9 14.6 1.0
HG21 A:ILE168 4.9 14.0 1.0
HA A:DTV303 5.0 27.2 0.8
O3 A:DTV303 5.0 24.0 0.8

Reference:

H.M.Wahba, L.Lecoq, M.Stevenson, A.Mansour, L.Cappadocia, J.Lafrance-Vanasse, K.J.Wilkinson, J.Sygusch, D.E.Wilcox, J.G.Omichinski. Structural and Biochemical Characterization of A Copper-Binding Mutant of the Organomercurial Lyase Merb: Insight Into the Key Role of the Active Site Aspartic Acid in Hg-Carbon Bond Cleavage and Metal Binding Specificity. Biochemistry V. 55 1070 2016.
ISSN: ISSN 0006-2960
PubMed: 26820485
DOI: 10.1021/ACS.BIOCHEM.5B01298
Page generated: Sun Dec 13 19:12:17 2020

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