Atomistry » Zinc » PDB 3tem-3ttd » 3tob
Atomistry »
  Zinc »
    PDB 3tem-3ttd »
      3tob »

Zinc in PDB 3tob: Human Mof E350Q Crystal Structure with Active Site Lysine Partially Acetylated

Enzymatic activity of Human Mof E350Q Crystal Structure with Active Site Lysine Partially Acetylated

All present enzymatic activity of Human Mof E350Q Crystal Structure with Active Site Lysine Partially Acetylated:
2.3.1.48;

Protein crystallography data

The structure of Human Mof E350Q Crystal Structure with Active Site Lysine Partially Acetylated, PDB code: 3tob 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) 34.52 / 2.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.971, 58.042, 120.338, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 25.3

Other elements in 3tob:

The structure of Human Mof E350Q Crystal Structure with Active Site Lysine Partially Acetylated also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Mof E350Q Crystal Structure with Active Site Lysine Partially Acetylated (pdb code 3tob). 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 Human Mof E350Q Crystal Structure with Active Site Lysine Partially Acetylated, PDB code: 3tob:

Zinc binding site 1 out of 1 in 3tob

Go back to Zinc Binding Sites List in 3tob
Zinc binding site 1 out of 1 in the Human Mof E350Q Crystal Structure with Active Site Lysine Partially Acetylated


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Mof E350Q Crystal Structure with Active Site Lysine Partially Acetylated within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:34.6
occ:1.00
NE2 A:HIS226 2.2 19.1 1.0
SG A:CYS213 2.3 18.6 1.0
SG A:CYS210 2.3 21.8 1.0
SG A:CYS230 2.4 22.0 1.0
CE1 A:HIS226 3.0 18.3 1.0
CB A:CYS210 3.1 19.5 1.0
CD2 A:HIS226 3.2 19.1 1.0
CB A:CYS213 3.3 19.1 1.0
CB A:CYS230 3.3 25.8 1.0
N A:CYS213 4.0 20.4 1.0
ND1 A:HIS226 4.1 20.8 1.0
CA A:CYS213 4.2 20.6 1.0
CG A:HIS226 4.3 20.7 1.0
CA A:CYS210 4.6 19.7 1.0
CA A:CYS230 4.7 27.1 1.0
CB A:LYS215 4.9 18.9 1.0
C A:CYS213 4.9 20.1 1.0
N A:LEU214 5.0 17.7 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: Wed Dec 16 04:52:29 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy