Atomistry » Zinc » PDB 2geh-2gzg » 2gfo
Atomistry »
  Zinc »
    PDB 2geh-2gzg »
      2gfo »

Zinc in PDB 2gfo: Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-Terminal Hydrolase 8

Enzymatic activity of Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-Terminal Hydrolase 8

All present enzymatic activity of Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-Terminal Hydrolase 8:
3.1.2.15;

Protein crystallography data

The structure of Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-Terminal Hydrolase 8, PDB code: 2gfo was solved by J.R.Walker, G.V.Avvakumov, S.Xue, E.M.Newman, P.J.Finerty Jr., C.Butler-Cole, J.Weigelt, M.Sundstrom, C.Arrowsmith, A.Edwards, A.Bochkarev, 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) 18.20 / 2.00
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 67.173, 67.173, 194.458, 90.00, 90.00, 120.00
R / Rfree (%) 16.8 / 21

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-Terminal Hydrolase 8 (pdb code 2gfo). 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 Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-Terminal Hydrolase 8, PDB code: 2gfo:

Zinc binding site 1 out of 1 in 2gfo

Go back to Zinc Binding Sites List in 2gfo
Zinc binding site 1 out of 1 in the Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-Terminal Hydrolase 8


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-Terminal Hydrolase 8 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1200

b:43.2
occ:1.00
SG A:CYS936 2.3 36.0 1.0
SG A:CYS939 2.3 35.1 1.0
SG A:CYS988 2.4 42.4 1.0
SG A:CYS985 2.4 39.2 1.0
CB A:CYS936 3.1 35.1 1.0
CB A:CYS985 3.2 35.4 1.0
CB A:CYS939 3.4 35.2 1.0
CB A:CYS988 3.5 41.8 1.0
N A:CYS939 3.7 34.0 1.0
N A:CYS988 3.9 40.7 1.0
CA A:CYS939 4.1 33.7 1.0
CA A:CYS988 4.3 40.6 1.0
CG A:ARG992 4.3 41.3 1.0
CD2 A:HIS987 4.5 36.2 1.0
CA A:CYS936 4.6 35.8 1.0
CB A:HIS987 4.6 40.3 1.0
CB A:THR938 4.7 35.1 1.0
CA A:CYS985 4.7 41.0 1.0
CD A:ARG992 4.7 40.2 1.0
NE A:ARG992 4.8 40.7 1.0
C A:THR938 4.8 37.9 1.0
C A:CYS939 4.8 33.9 1.0
C A:HIS987 4.9 41.6 1.0
CG A:HIS987 4.9 42.4 1.0
N A:HIS940 4.9 34.7 1.0

Reference:

G.V.Avvakumov, J.R.Walker, S.Xue, P.J.Finerty Jr., F.Mackenzie, E.M.Newman, S.Dhe-Paganon. Amino-Terminal Dimerization, NRDP1-Rhodanese Interaction, and Inhibited Catalytic Domain Conformation of the Ubiquitin-Specific Protease 8 (USP8). J.Biol.Chem. V. 281 38061 2006.
ISSN: ISSN 0021-9258
PubMed: 17035239
DOI: 10.1074/JBC.M606704200
Page generated: Thu Oct 17 00:18:30 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy