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Zinc in PDB 3ehv: X-Ray Structure of Human Ubiquitin Zn(II) Adduct

Enzymatic activity of X-Ray Structure of Human Ubiquitin Zn(II) Adduct

All present enzymatic activity of X-Ray Structure of Human Ubiquitin Zn(II) Adduct:
6.3.2.19;

Protein crystallography data

The structure of X-Ray Structure of Human Ubiquitin Zn(II) Adduct, PDB code: 3ehv was solved by G.Falini, S.Fermani, G.Tosi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.15 / 1.81
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.357, 50.946, 93.317, 90.00, 90.00, 90.00
R / Rfree (%) 22.2 / 27.1

Zinc Binding Sites:

The binding sites of Zinc atom in the X-Ray Structure of Human Ubiquitin Zn(II) Adduct (pdb code 3ehv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the X-Ray Structure of Human Ubiquitin Zn(II) Adduct, PDB code: 3ehv:

Zinc binding site 1 out of 1 in 3ehv

Go back to Zinc Binding Sites List in 3ehv
Zinc binding site 1 out of 1 in the X-Ray Structure of Human Ubiquitin Zn(II) Adduct


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Structure of Human Ubiquitin Zn(II) Adduct within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn101

b:44.1
occ:0.50
NE2 B:HIS68 2.4 38.0 1.0
NE2 A:HIS68 2.5 34.7 1.0
O B:HOH130 2.8 60.1 0.5
CE1 A:HIS68 2.8 34.5 1.0
CE1 B:HIS68 3.0 37.9 1.0
O A:HOH102 3.2 48.3 0.5
CD2 B:HIS68 3.6 36.4 1.0
CD2 A:HIS68 3.9 32.7 1.0
CE A:LYS6 3.9 38.5 1.0
ND1 A:HIS68 4.1 33.6 1.0
ND1 B:HIS68 4.2 36.3 1.0
CD A:LYS6 4.3 37.6 1.0
CG B:HIS68 4.5 34.4 1.0
CG2 A:THR66 4.7 25.4 1.0
CG A:HIS68 4.7 30.6 1.0
NZ A:LYS6 4.7 40.9 1.0
O A:HOH114 4.7 45.7 1.0
CD B:LYS6 4.8 40.1 1.0
O A:HOH132 5.0 69.1 1.0

Reference:

G.Falini, S.Fermani, G.Tosi, F.Arnesano, G.Natile. Structural Probing of Zn(II), Cd(II) and Hg(II) Binding to Human Ubiquitin. Chem.Commun.(Camb.) V. 45 5960 2008.
ISSN: ISSN 1359-7345
PubMed: 19030552
DOI: 10.1039/B813463D
Page generated: Wed Dec 16 04:16:13 2020

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