Atomistry » Arsenic » PDB 3sr6-4cx0 » 3to7
Atomistry »
  Arsenic »
    PDB 3sr6-4cx0 »
      3to7 »

Arsenic in PDB 3to7: Crystal Structure of Yeast ESA1 Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated

Enzymatic activity of Crystal Structure of Yeast ESA1 Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated

All present enzymatic activity of Crystal Structure of Yeast ESA1 Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated:
2.3.1.48;

Protein crystallography data

The structure of Crystal Structure of Yeast ESA1 Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated, PDB code: 3to7 was solved by H.Yuan, E.C.Ding, R.Marmorstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.51 / 1.90
Space group I 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 183.040, 183.040, 183.040, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 22.6

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of Yeast ESA1 Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated (pdb code 3to7). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Crystal Structure of Yeast ESA1 Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated, PDB code: 3to7:

Arsenic binding site 1 out of 1 in 3to7

Go back to Arsenic Binding Sites List in 3to7
Arsenic binding site 1 out of 1 in the Crystal Structure of Yeast ESA1 Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of Yeast ESA1 Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As501

b:20.0
occ:1.00
 AS A:CAD501 0.0 20.0 1.0
C2 A:CAD501 1.9 20.0 1.0
C1 A:CAD501 2.0 20.0 1.0
O A:HOH466 4.0 19.8 1.0
CB A:CYS304 4.2 13.0 1.0
CG2 A:THR263 4.3 13.9 1.0
O A:ALA303 4.3 13.6 1.0
CG A:ALY262 4.3 11.3 1.0
N A:THR263 4.4 14.3 1.0
C A:ALA303 4.5 11.6 1.0
OE2 A:GLU338 4.6 16.0 1.0
OE1 A:GLU338 4.7 20.9 1.0
CA A:ALY262 4.7 12.5 1.0
N A:CYS304 4.8 10.5 1.0
CD A:GLU338 4.8 24.1 1.0
SG A:CYS304 4.9 20.7 1.0
CB A:THR263 4.9 18.0 1.0
CA A:CYS304 4.9 14.3 1.0
CB A:ALA303 5.0 12.1 1.0

Reference:

H.Yuan, D.Rossetto, H.Mellert, W.Dang, M.Srinivasan, J.Johnson, S.Hodawadekar, E.C.Ding, K.Speicher, N.Abshiru, R.Perry, J.Wu, C.Yang, Y.G.Zheng, D.W.Speicher, P.Thibault, A.Verreault, F.B.Johnson, S.L.Berger, R.Sternglanz, S.B.Mcmahon, J.Cote, R.Marmorstein. Myst Protein Acetyltransferase Activity Requires Active Site Lysine Autoacetylation. Embo J. V. 31 58 2011.
ISSN: ISSN 0261-4189
PubMed: 22020126
DOI: 10.1038/EMBOJ.2011.382
Page generated: Sat Dec 12 01:42:01 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy