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Zinc in PDB 3v6e: Crystal Structure of USP2 and A Mutant Form of Ubiquitin

Enzymatic activity of Crystal Structure of USP2 and A Mutant Form of Ubiquitin

All present enzymatic activity of Crystal Structure of USP2 and A Mutant Form of Ubiquitin:
3.4.19.12;

Protein crystallography data

The structure of Crystal Structure of USP2 and A Mutant Form of Ubiquitin, PDB code: 3v6e was solved by M.Neculai, A.Ernst, S.Sidhu, C.H.Arrowsmith, A.M.Edwards, C.Bountra, J.Weigelt, S.Dhe-Paganon, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.06 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.097, 84.124, 87.371, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 23.4

Other elements in 3v6e:

The structure of Crystal Structure of USP2 and A Mutant Form of Ubiquitin also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of USP2 and A Mutant Form of Ubiquitin (pdb code 3v6e). 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 Crystal Structure of USP2 and A Mutant Form of Ubiquitin, PDB code: 3v6e:

Zinc binding site 1 out of 1 in 3v6e

Go back to Zinc Binding Sites List in 3v6e
Zinc binding site 1 out of 1 in the Crystal Structure of USP2 and A Mutant Form of Ubiquitin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of USP2 and A Mutant Form of Ubiquitin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn700

b:18.6
occ:1.00
SG A:CYS428 2.3 14.2 1.0
SG A:CYS476 2.3 19.9 1.0
SG A:CYS425 2.3 14.7 1.0
SG A:CYS479 2.4 20.5 1.0
CB A:CYS425 3.1 13.3 1.0
CB A:CYS428 3.3 15.7 1.0
CB A:CYS476 3.4 21.4 1.0
CB A:CYS479 3.4 25.2 1.0
N A:CYS428 3.6 15.8 1.0
N A:CYS479 3.8 26.6 1.0
CA A:CYS428 4.1 15.3 1.0
CA A:CYS479 4.2 25.9 1.0
CB A:ARG478 4.3 27.1 1.0
CG A:LYS483 4.4 20.7 1.0
CB A:ASP427 4.5 18.1 1.0
CA A:CYS425 4.6 13.6 1.0
C A:ASP427 4.8 17.1 1.0
C A:ARG478 4.8 27.3 1.0
CA A:CYS476 4.8 21.7 1.0
C A:CYS428 4.9 14.9 1.0
CG A:ARG478 5.0 27.4 1.0
N A:GLY429 5.0 14.8 1.0
CA A:ARG478 5.0 27.2 1.0
CA A:ASP427 5.0 17.4 1.0

Reference:

A.Ernst, G.Avvakumov, J.Tong, Y.Fan, Y.Zhao, P.Alberts, A.Persaud, J.R.Walker, A.M.Neculai, D.Neculai, A.Vorobyov, P.Garg, L.Beatty, P.K.Chan, Y.C.Juang, M.C.Landry, C.Yeh, E.Zeqiraj, K.Karamboulas, A.Allali-Hassani, M.Vedadi, M.Tyers, J.Moffat, F.Sicheri, L.Pelletier, D.Durocher, B.Raught, D.Rotin, J.Yang, M.F.Moran, S.Dhe-Paganon, S.S.Sidhu. A Strategy For Modulation of Enzymes in the Ubiquitin System. Science V. 339 590 2013.
ISSN: ISSN 0036-8075
PubMed: 23287719
DOI: 10.1126/SCIENCE.1230161
Page generated: Sat Oct 26 17:35:24 2024

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