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Arsenic in PDB 3to9: Crystal Structure of Yeast ESA1 E338Q Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated

Enzymatic activity of Crystal Structure of Yeast ESA1 E338Q Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated

All present enzymatic activity of Crystal Structure of Yeast ESA1 E338Q 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 E338Q Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated, PDB code: 3to9 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) 43.01 / 2.00
Space group I 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 182.470, 182.470, 182.470, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 23.4

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of Yeast ESA1 E338Q Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated (pdb code 3to9). 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 E338Q Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated, PDB code: 3to9:

Arsenic binding site 1 out of 1 in 3to9

Go back to Arsenic Binding Sites List in 3to9
Arsenic binding site 1 out of 1 in the Crystal Structure of Yeast ESA1 E338Q 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 E338Q Hat Domain Bound to Coenzyme A with Active Site Lysine Acetylated within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As502

b:51.0
occ:1.00
 AS A:CAD502 0.0 51.0 1.0
C1 A:CAD502 2.0 26.9 1.0
C2 A:CAD502 2.0 25.9 1.0
CB A:CYS304 4.0 20.6 1.0
CG2 A:THR263 4.2 23.9 1.0
O A:HOH479 4.2 27.3 1.0
O A:ALA303 4.3 20.7 1.0
C A:ALA303 4.3 19.7 1.0
CH A:ALY262 4.3 20.6 1.0
NE2 A:GLN338 4.3 25.9 1.0
CG A:ALY262 4.3 21.1 1.0
CB A:ALA303 4.3 18.8 1.0
CH3 A:ALY262 4.4 19.9 1.0
N A:CYS304 4.4 18.6 1.0
NZ A:ALY262 4.4 19.8 1.0
N A:THR263 4.5 22.6 1.0
OE1 A:GLN338 4.5 22.7 1.0
OH A:ALY262 4.6 19.1 1.0
CA A:CYS304 4.7 19.2 1.0
CD A:GLN338 4.8 24.3 1.0
CB A:THR263 4.8 25.0 1.0
CA A:ALA303 4.9 18.7 1.0
CA A:ALY262 5.0 22.0 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: Sun Jul 6 23:34:08 2025

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