Atomistry » Zinc » PDB 5ofa-5on3 » 5ohk
Atomistry »
  Zinc »
    PDB 5ofa-5on3 »
      5ohk »

Zinc in PDB 5ohk: Crystal Structure of USP30 in Covalent Complex with Ubiquitin Propargylamide (High Resolution)

Enzymatic activity of Crystal Structure of USP30 in Covalent Complex with Ubiquitin Propargylamide (High Resolution)

All present enzymatic activity of Crystal Structure of USP30 in Covalent Complex with Ubiquitin Propargylamide (High Resolution):
3.4.19.12;

Protein crystallography data

The structure of Crystal Structure of USP30 in Covalent Complex with Ubiquitin Propargylamide (High Resolution), PDB code: 5ohk was solved by M.Gersch, D.Komander, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 67.35 / 2.34
Space group P 21 2 21
Cell size a, b, c (Å), α, β, γ (°) 50.917, 94.408, 96.115, 90.00, 90.00, 90.00
R / Rfree (%) 22.9 / 26.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of USP30 in Covalent Complex with Ubiquitin Propargylamide (High Resolution) (pdb code 5ohk). 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 USP30 in Covalent Complex with Ubiquitin Propargylamide (High Resolution), PDB code: 5ohk:

Zinc binding site 1 out of 1 in 5ohk

Go back to Zinc Binding Sites List in 5ohk
Zinc binding site 1 out of 1 in the Crystal Structure of USP30 in Covalent Complex with Ubiquitin Propargylamide (High Resolution)


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 USP30 in Covalent Complex with Ubiquitin Propargylamide (High Resolution) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:96.6
occ:1.00
 SG A:CYS237 2.3 81.3 1.0
SG A:CYS284 2.4 77.9 1.0
SG A:CYS287 2.4 82.8 1.0
SG A:CYS234 2.4 75.4 1.0
CB A:CYS234 3.0 73.8 1.0
CB A:CYS237 3.4 69.8 1.0
CB A:CYS284 3.4 76.7 1.0
CB A:CYS287 3.7 81.3 1.0
N A:CYS287 3.8 86.5 1.0
N A:CYS237 3.9 73.0 1.0
CB A:ASN286 4.2 86.2 1.0
CA A:CYS237 4.2 76.0 1.0
CA A:CYS287 4.4 91.6 1.0
CA A:CYS234 4.5 73.3 1.0
CG2 A:THR306 4.6 79.5 1.0
CB A:HIS236 4.6 80.7 1.0
C A:ASN286 4.8 88.1 1.0
CA A:CYS284 4.8 89.8 1.0
CA A:ASN286 4.9 88.8 1.0
N A:ASN286 4.9 94.2 1.0
C A:HIS236 4.9 79.8 1.0
C A:CYS237 5.0 82.2 1.0

Reference:

M.Gersch, C.Gladkova, A.F.Schubert, M.A.Michel, S.Maslen, D.Komander. Mechanism and Regulation of the LYS6-Selective Deubiquitinase USP30. Nat. Struct. Mol. Biol. V. 24 920 2017.
ISSN: ESSN 1545-9985
PubMed: 28945249
DOI: 10.1038/NSMB.3475
Page generated: Sun Oct 27 23:37:09 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy