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Mercury in PDB 5w2l: Structure of A Central Domain of Human CTC1

Protein crystallography data

The structure of Structure of A Central Domain of Human CTC1, PDB code: 5w2l was solved by C.Rice, E.Skordalakes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.86 / 1.86
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.537, 50.776, 144.538, 90.00, 90.00, 90.00
R / Rfree (%) 20.9 / 24.9

Mercury Binding Sites:

The binding sites of Mercury atom in the Structure of A Central Domain of Human CTC1 (pdb code 5w2l). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 6 binding sites of Mercury where determined in the Structure of A Central Domain of Human CTC1, PDB code: 5w2l:
Jump to Mercury binding site number: 1; 2; 3; 4; 5; 6;

Mercury binding site 1 out of 6 in 5w2l

Go back to Mercury Binding Sites List in 5w2l
Mercury binding site 1 out of 6 in the Structure of A Central Domain of Human CTC1


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structure of A Central Domain of Human CTC1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg901

b:0.8
occ:0.80
SG A:CYS848 2.4 74.4 1.0
ND1 A:HIS797 2.6 43.4 1.0
SG A:CYS851 3.0 46.0 1.0
O A:SER850 3.2 50.0 1.0
CG A:HIS797 3.2 38.9 1.0
CB A:HIS797 3.3 34.4 1.0
C A:SER850 3.3 48.3 1.0
CB A:CYS848 3.4 61.7 1.0
N A:CYS851 3.6 45.0 1.0
CE1 A:HIS797 3.6 43.9 1.0
N A:SER850 3.7 52.5 1.0
CA A:CYS851 3.9 41.6 1.0
CA A:SER850 4.0 50.3 1.0
CB A:CYS851 4.1 43.5 1.0
N A:HIS797 4.2 29.7 1.0
OG A:SER850 4.2 56.2 1.0
CA A:HIS797 4.3 30.3 1.0
CD2 A:HIS797 4.4 41.4 1.0
C A:CYS848 4.4 51.1 1.0
N A:ALA849 4.5 49.3 1.0
CA A:CYS848 4.5 55.5 1.0
NE2 A:HIS797 4.5 45.4 1.0
O A:CYS848 4.8 48.0 1.0
CB A:SER850 4.8 54.5 1.0
C A:ALA849 4.9 54.8 1.0
CD2 A:LEU845 4.9 36.9 1.0

Mercury binding site 2 out of 6 in 5w2l

Go back to Mercury Binding Sites List in 5w2l
Mercury binding site 2 out of 6 in the Structure of A Central Domain of Human CTC1


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Structure of A Central Domain of Human CTC1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg902

b:45.9
occ:0.74
OE1 A:GLU777 2.1 29.6 1.0
NE2 A:HIS726 2.2 35.9 1.0
CD A:GLU777 3.1 32.1 1.0
CD2 A:HIS726 3.1 33.5 1.0
CE1 A:HIS726 3.2 37.3 1.0
OE2 A:GLU777 3.4 31.8 1.0
NH2 A:ARG775 3.9 42.4 1.0
CG A:HIS726 4.2 36.6 1.0
ND1 A:HIS726 4.2 35.7 1.0
CG A:GLU777 4.4 28.9 1.0
CA A:GLU777 4.6 30.1 1.0
CB A:GLU777 4.6 29.4 1.0
CZ A:ARG775 4.8 41.9 1.0

Mercury binding site 3 out of 6 in 5w2l

Go back to Mercury Binding Sites List in 5w2l
Mercury binding site 3 out of 6 in the Structure of A Central Domain of Human CTC1


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Structure of A Central Domain of Human CTC1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg903

b:30.9
occ:0.23
NE2 A:HIS737 2.1 30.5 1.0
OE1 A:GLU739 2.2 31.0 1.0
CD A:GLU739 2.9 31.1 1.0
OE2 A:GLU739 3.0 29.6 1.0
CD2 A:HIS737 3.0 30.4 1.0
CE1 A:HIS737 3.1 32.1 1.0
O A:HOH1015 4.0 46.0 1.0
ND1 A:HIS737 4.2 30.4 1.0
CG A:HIS737 4.2 30.2 1.0
CG A:GLU739 4.4 31.4 1.0
CA A:GLU739 4.6 27.0 1.0
CB A:GLU739 4.9 28.9 1.0
O A:LYS738 5.0 27.0 1.0

Mercury binding site 4 out of 6 in 5w2l

Go back to Mercury Binding Sites List in 5w2l
Mercury binding site 4 out of 6 in the Structure of A Central Domain of Human CTC1


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Structure of A Central Domain of Human CTC1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg901

b:57.5
occ:0.23
SG B:CYS848 2.0 72.7 1.0
SG B:CYS851 2.3 45.4 1.0
ND1 B:HIS797 2.4 42.2 1.0
O B:SER850 2.4 44.9 1.0
C B:SER850 2.9 46.8 1.0
CB B:CYS848 3.0 61.0 1.0
CG B:HIS797 3.1 38.9 1.0
CB B:HIS797 3.2 33.8 1.0
N B:CYS851 3.3 43.5 1.0
CE1 B:HIS797 3.5 40.5 1.0
CB B:CYS851 3.5 42.6 1.0
CA B:CYS851 3.5 41.5 1.0
N B:SER850 3.8 49.5 1.0
CA B:SER850 3.8 49.5 1.0
N B:HIS797 4.1 31.7 1.0
CA B:HIS797 4.2 30.6 1.0
CD2 B:HIS797 4.3 39.7 1.0
CA B:CYS848 4.3 58.4 1.0
C B:CYS848 4.4 55.1 1.0
NE2 B:HIS797 4.4 41.0 1.0
CB B:SER850 4.6 49.7 1.0
N B:ALA849 4.7 54.6 1.0
O B:CYS848 4.7 55.7 1.0
O B:HIS797 4.9 30.9 1.0
C B:ALA849 4.9 54.1 1.0
C B:CYS851 5.0 41.8 1.0

Mercury binding site 5 out of 6 in 5w2l

Go back to Mercury Binding Sites List in 5w2l
Mercury binding site 5 out of 6 in the Structure of A Central Domain of Human CTC1


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 5 of Structure of A Central Domain of Human CTC1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg902

b:0.6
occ:0.11
SG B:CYS736 2.0 32.1 1.0
ND1 B:HIS737 2.4 29.3 1.0
CB B:CYS736 3.2 31.3 1.0
CE1 B:HIS737 3.3 29.9 1.0
CG B:HIS737 3.4 29.0 1.0
CB B:HIS737 3.6 27.7 1.0
C B:CYS736 3.6 28.9 1.0
N B:HIS737 3.8 27.5 1.0
O B:CYS736 3.9 27.8 1.0
CA B:CYS736 4.0 28.0 1.0
CA B:HIS737 4.3 27.1 1.0
NE2 B:HIS737 4.4 29.2 1.0
CD2 B:LEU766 4.4 35.9 1.0
CD2 B:HIS737 4.5 28.9 1.0
O B:HOH1042 4.6 33.2 1.0

Mercury binding site 6 out of 6 in 5w2l

Go back to Mercury Binding Sites List in 5w2l
Mercury binding site 6 out of 6 in the Structure of A Central Domain of Human CTC1


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 6 of Structure of A Central Domain of Human CTC1 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg903

b:27.8
occ:0.15
NE2 B:HIS726 2.0 30.5 1.0
OE2 B:GLU777 2.1 38.0 1.0
CD B:GLU777 2.9 34.1 1.0
CE1 B:HIS726 2.9 32.6 1.0
CD2 B:HIS726 3.1 30.3 1.0
OE1 B:GLU777 3.1 35.8 1.0
O B:HOH1026 4.0 38.0 1.0
ND1 B:HIS726 4.1 32.6 1.0
CG B:HIS726 4.2 31.6 1.0
CG B:GLU777 4.4 37.8 1.0
CG B:PRO725 4.5 44.4 1.0

Reference:

P.K.Shastrula, C.T.Rice, Z.Wang, P.M.Lieberman, E.Skordalakes. Structural and Functional Analysis of An Ob-Fold in Human CTC1 Implicated in Telomere Maintenance and Bone Marrow Syndromes. Nucleic Acids Res. V. 46 972 2018.
ISSN: ESSN 1362-4962
PubMed: 29228254
DOI: 10.1093/NAR/GKX1213
Page generated: Sun Dec 13 19:13:20 2020

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