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Zinc in PDB 2hd5: USP2 in Complex with Ubiquitin

Enzymatic activity of USP2 in Complex with Ubiquitin

All present enzymatic activity of USP2 in Complex with Ubiquitin:
3.1.2.15;

Protein crystallography data

The structure of USP2 in Complex with Ubiquitin, PDB code: 2hd5 was solved by M.Renatus, M.Kroemer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.47 / 1.85
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 106.903, 45.534, 76.360, 90.00, 110.01, 90.00
R / Rfree (%) 17.7 / 22.9

Zinc Binding Sites:

The binding sites of Zinc atom in the USP2 in Complex with Ubiquitin (pdb code 2hd5). 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 USP2 in Complex with Ubiquitin, PDB code: 2hd5:

Zinc binding site 1 out of 1 in 2hd5

Go back to Zinc Binding Sites List in 2hd5
Zinc binding site 1 out of 1 in the USP2 in Complex with Ubiquitin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of USP2 in Complex with Ubiquitin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:21.1
occ:1.00
SG A:CYS337 2.3 17.8 1.0
SG A:CYS381 2.4 22.7 1.0
SG A:CYS384 2.4 24.3 1.0
SG A:CYS334 2.5 17.1 1.0
CB A:CYS334 3.1 14.8 1.0
CB A:CYS381 3.2 23.7 1.0
CB A:CYS384 3.2 23.4 1.0
CB A:CYS337 3.2 18.9 1.0
N A:CYS384 3.5 26.4 1.0
N A:CYS337 3.7 17.3 1.0
CA A:CYS384 4.0 26.1 1.0
CA A:CYS337 4.1 16.8 1.0
CB A:ARG383 4.4 30.0 1.0
CA A:CYS334 4.6 14.6 1.0
CB A:ASP336 4.6 23.3 1.0
C A:ARG383 4.6 28.8 1.0
CA A:CYS381 4.7 23.7 1.0
C A:CYS337 4.8 17.1 1.0
C A:ASP336 4.8 20.3 1.0
N A:GLY338 4.9 15.7 1.0
CG A:LYS387 4.9 30.2 1.0
CA A:ARG383 4.9 29.2 1.0

Reference:

M.Renatus, S.G.Parrado, A.D'arcy, U.Eidhoff, B.Gerhartz, U.Hassiepen, B.Pierrat, R.Riedl, D.Vinzenz, S.Worpenberg, M.Kroemer. Structural Basis of Ubiquitin Recognition By the Deubiquitinating Protease USP2. Structure V. 14 1293 2006.
ISSN: ISSN 0969-2126
PubMed: 16905103
DOI: 10.1016/J.STR.2006.06.012
Page generated: Wed Dec 16 03:30:08 2020

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