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Mercury in PDB 5fta: Crystal Structure of the N-Terminal Btb Domain of Human KCTD10

Protein crystallography data

The structure of Crystal Structure of the N-Terminal Btb Domain of Human KCTD10, PDB code: 5fta was solved by D.M.Pinkas, C.E.Sanvitale, N.Solcan, S.Goubin, C.Tallant, J.A.Newman, J.Kopec, F.Fitzpatrick, R.Talon, P.Collins, T.Krojer, F.Von Delft, C.H.Arrowsmith, A.M.Edwards, C.Bountra, A.Bullock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.77 / 2.64
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.150, 83.660, 58.680, 90.00, 95.18, 90.00
R / Rfree (%) 22.6 / 25.8

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of the N-Terminal Btb Domain of Human KCTD10 (pdb code 5fta). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 4 binding sites of Mercury where determined in the Crystal Structure of the N-Terminal Btb Domain of Human KCTD10, PDB code: 5fta:
Jump to Mercury binding site number: 1; 2; 3; 4;

Mercury binding site 1 out of 4 in 5fta

Go back to Mercury Binding Sites List in 5fta
Mercury binding site 1 out of 4 in the Crystal Structure of the N-Terminal Btb Domain of Human KCTD10


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 N-Terminal Btb Domain of Human KCTD10 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg1131

b:81.2
occ:0.60
SG A:CYS80 2.5 47.6 1.0
HB3 A:CYS80 2.7 57.2 1.0
CB A:CYS80 3.0 47.7 1.0
HB2 A:CYS80 3.3 57.2 1.0
HB2 A:LYS82 3.4 48.4 1.0
HB3 A:LYS82 3.6 48.4 1.0
HD3 A:LYS82 3.8 53.6 1.0
CB A:LYS82 4.0 40.4 1.0
HD2 A:LYS82 4.0 53.6 1.0
H A:LYS82 4.2 47.7 1.0
CD A:LYS82 4.3 44.7 1.0
CA A:CYS80 4.5 46.7 1.0
CG A:LYS82 4.8 39.6 1.0
O A:HOH2005 4.8 43.3 1.0
C A:CYS80 4.9 46.8 1.0
HA A:CYS80 4.9 56.0 1.0
N A:LYS82 4.9 39.8 1.0
HD2 A:HIS83 4.9 51.4 1.0

Mercury binding site 2 out of 4 in 5fta

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Mercury binding site 2 out of 4 in the Crystal Structure of the N-Terminal Btb Domain of Human KCTD10


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 N-Terminal Btb Domain of Human KCTD10 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Hg1131

b:58.9
occ:0.83
SG B:CYS80 2.4 32.0 1.0
HD22 A:ASN89 2.8 41.2 1.0
ND2 A:ASN89 3.3 34.3 1.0
HB2 B:CYS80 3.4 30.5 1.0
CB B:CYS80 3.5 25.4 1.0
HD21 A:ASN89 3.5 41.2 1.0
HB2 B:LYS82 3.5 37.6 1.0
HA3 A:GLY85 3.6 35.2 1.0
HB3 B:CYS80 3.6 30.5 1.0
HD2 B:LYS82 3.9 44.6 1.0
HB3 B:LYS82 3.9 37.6 1.0
O A:GLY85 4.0 36.7 1.0
HD3 B:LYS82 4.0 44.6 1.0
C A:GLY85 4.1 28.9 1.0
CB B:LYS82 4.2 31.4 1.0
CA A:GLY85 4.3 29.3 1.0
CG A:ASN89 4.3 30.5 1.0
CD B:LYS82 4.4 37.2 1.0
H B:LYS82 4.6 43.6 1.0
N A:THR86 4.6 40.8 1.0
HA A:THR86 4.6 45.6 1.0
HA2 A:GLY85 4.6 35.2 1.0
OD1 A:ASN89 4.7 32.9 1.0
CA B:CYS80 4.8 30.1 1.0
CG B:LYS82 4.9 33.7 1.0
H A:THR86 4.9 48.9 1.0
HA B:CYS80 5.0 36.1 1.0

Mercury binding site 3 out of 4 in 5fta

Go back to Mercury Binding Sites List in 5fta
Mercury binding site 3 out of 4 in the Crystal Structure of the N-Terminal Btb Domain of Human KCTD10


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Crystal Structure of the N-Terminal Btb Domain of Human KCTD10 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Hg1129

b:56.7
occ:0.61
SG C:CYS80 2.4 49.2 1.0
HB2 C:LYS82 3.2 50.0 1.0
OD1 B:ASP93 3.3 39.6 1.0
HD2 C:LYS82 3.5 58.0 1.0
HD3 C:LYS82 3.6 58.0 1.0
CB C:CYS80 3.6 50.6 1.0
O C:HOH2006 3.6 33.9 1.0
HB3 C:LYS82 3.6 50.0 1.0
CG B:ASP93 3.7 44.4 1.0
HB2 C:CYS80 3.7 60.7 1.0
HB3 C:CYS80 3.7 60.7 1.0
HB3 B:ASP93 3.8 49.8 1.0
CB C:LYS82 3.9 41.7 1.0
HA B:ASP93 3.9 53.3 1.0
CD C:LYS82 3.9 48.3 1.0
CB B:ASP93 4.2 41.5 1.0
OD2 B:ASP93 4.2 47.0 1.0
H C:LYS82 4.4 50.9 1.0
CG C:LYS82 4.5 44.8 1.0
CA B:ASP93 4.6 44.4 1.0
CA C:CYS80 5.0 45.4 1.0

Mercury binding site 4 out of 4 in 5fta

Go back to Mercury Binding Sites List in 5fta
Mercury binding site 4 out of 4 in the Crystal Structure of the N-Terminal Btb Domain of Human KCTD10


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Crystal Structure of the N-Terminal Btb Domain of Human KCTD10 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Hg1131

b:58.9
occ:0.71
SG D:CYS80 2.5 48.0 1.0
HD22 C:ASN89 2.8 49.3 1.0
ND2 C:ASN89 3.4 41.0 1.0
HB2 D:LYS82 3.5 54.2 1.0
HA3 C:GLY85 3.5 45.8 1.0
HB2 D:CYS80 3.5 43.0 1.0
CB D:CYS80 3.5 35.9 1.0
HD21 C:ASN89 3.6 49.3 1.0
HB3 D:CYS80 3.6 43.0 1.0
HB3 D:LYS82 3.9 54.2 1.0
O C:GLY85 3.9 41.9 1.0
HD2 D:LYS82 3.9 55.9 1.0
C C:GLY85 4.0 38.9 1.0
HD3 D:LYS82 4.0 55.9 1.0
CB D:LYS82 4.1 45.2 1.0
CA C:GLY85 4.2 38.2 1.0
O C:HOH2004 4.2 36.6 1.0
CG C:ASN89 4.3 44.7 1.0
CD D:LYS82 4.4 46.6 1.0
HA2 C:GLY85 4.5 45.8 1.0
H D:LYS82 4.5 43.9 1.0
N C:THR86 4.6 45.8 1.0
HA C:THR86 4.6 57.2 1.0
OD1 C:ASN89 4.6 44.8 1.0
CG D:LYS82 4.9 46.7 1.0
CA D:CYS80 4.9 36.2 1.0
H C:THR86 4.9 55.0 1.0

Reference:

D.M.Pinkas, C.E.Sanvitale, J.C.Bufton, F.J.Sorrell, N.Solcan, R.Chalk, J.Doutch, A.N.Bullock. Structural Complexity in the Kctd Family of CULLIN3-Dependent E3 Ubiquitin Ligases. Biochem. J. V. 474 3747 2017.
ISSN: ESSN 1470-8728
PubMed: 28963344
DOI: 10.1042/BCJ20170527
Page generated: Sun Dec 13 19:12:38 2020

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