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Zinc in PDB 7xv2: Trim E3 Ubiquitin Ligase

Protein crystallography data

The structure of Trim E3 Ubiquitin Ligase, PDB code: 7xv2 was solved by S.H.Park, H.K.Song, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.41 / 2.75
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 73.295, 110.171, 95.936, 90, 100.8, 90
R / Rfree (%) 20.5 / 25.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Trim E3 Ubiquitin Ligase (pdb code 7xv2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Trim E3 Ubiquitin Ligase, PDB code: 7xv2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7xv2

Go back to Zinc Binding Sites List in 7xv2
Zinc binding site 1 out of 2 in the Trim E3 Ubiquitin Ligase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Trim E3 Ubiquitin Ligase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:189.8
occ:1.00
SG A:CYS105 2.0 245.0 1.0
ND1 A:HIS89 2.0 233.6 1.0
SG A:CYS108 2.3 154.7 1.0
SG A:CYS86 2.4 140.8 1.0
CE1 A:HIS89 2.8 216.5 1.0
CB A:CYS105 3.0 193.1 1.0
CG A:HIS89 3.1 209.7 1.0
CB A:CYS108 3.4 139.8 1.0
N A:CYS108 3.5 136.6 1.0
CB A:HIS89 3.6 181.8 1.0
NE2 A:HIS89 4.0 217.2 1.0
OE1 A:GLU88 4.0 198.5 1.0
CA A:CYS108 4.0 128.3 1.0
CB A:CYS86 4.1 160.9 1.0
CA A:CYS105 4.1 148.9 1.0
N A:CYS105 4.1 129.1 1.0
CD2 A:HIS89 4.1 220.8 1.0
N A:HIS89 4.5 176.1 1.0
CB A:VAL107 4.6 122.9 1.0
C A:CYS105 4.6 129.7 1.0
C A:VAL107 4.6 143.3 1.0
CA A:HIS89 4.7 167.2 1.0
O A:CYS105 4.7 107.9 1.0
N A:VAL107 4.7 142.5 1.0
CA A:VAL107 4.9 139.4 1.0

Zinc binding site 2 out of 2 in 7xv2

Go back to Zinc Binding Sites List in 7xv2
Zinc binding site 2 out of 2 in the Trim E3 Ubiquitin Ligase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Trim E3 Ubiquitin Ligase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn502

b:106.7
occ:1.00
ND1 A:HIS117 2.0 135.1 1.0
ND1 A:HIS114 2.1 152.6 1.0
OD2 A:ASP100 2.2 188.2 1.0
SG A:CYS97 2.3 135.4 1.0
CE1 A:HIS117 2.6 124.4 1.0
CG A:HIS114 3.0 139.7 1.0
CG A:ASP100 3.1 161.6 1.0
CE1 A:HIS114 3.2 140.0 1.0
CB A:HIS114 3.2 123.7 1.0
CG A:HIS117 3.2 115.0 1.0
CB A:CYS97 3.4 119.2 1.0
CB A:ASP100 3.7 129.7 1.0
NE2 A:HIS117 3.8 124.4 1.0
CB A:HIS117 3.9 115.8 1.0
CA A:HIS114 3.9 129.8 1.0
OD1 A:ASP100 4.0 172.1 1.0
CD2 A:HIS117 4.1 123.3 1.0
CD2 A:HIS114 4.1 142.5 1.0
NE2 A:HIS114 4.2 135.1 1.0
CG A:GLN99 4.3 138.5 1.0
N A:ASP100 4.5 124.1 1.0
OE1 A:GLN99 4.6 140.7 1.0
CA A:ASP100 4.7 121.3 1.0
CA A:CYS97 4.8 107.6 1.0
CD A:GLN99 4.8 141.7 1.0
C A:HIS114 4.9 142.7 1.0
N A:HIS114 4.9 134.6 1.0
O A:HIS114 4.9 150.4 1.0

Reference:

S.H.Park, H.K.Song. Trim E3 Ubiquitin Ligase Mutant To Be Published.
Page generated: Wed Oct 30 15:18:06 2024

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