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

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

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

Protein crystallography data

The structure of Human Mof Crystal Structure with Active Site Lysine Partially Acetylated, PDB code: 3toa 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) 43.23 / 3.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.255, 58.534, 121.501, 90.00, 90.00, 90.00
R / Rfree (%) 24.6 / 26.5

Other elements in 3toa:

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

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

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

Zinc binding site 1 out of 1 in 3toa

Go back to Zinc Binding Sites List in 3toa
Zinc binding site 1 out of 1 in the Human Mof 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 Crystal Structure with Active Site Lysine Partially Acetylated within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:85.4
occ:1.00
 NE2 A:HIS226 2.3 62.3 1.0
SG A:CYS213 2.3 55.1 1.0
SG A:CYS210 2.4 57.9 1.0
SG A:CYS230 2.5 0.2 1.0
CB A:CYS213 3.1 55.2 1.0
CB A:CYS210 3.1 53.5 1.0
CE1 A:HIS226 3.2 61.1 1.0
CD2 A:HIS226 3.3 62.2 1.0
CB A:CYS230 3.6 0.5 1.0
N A:CYS213 3.7 57.5 1.0
CA A:CYS213 4.0 57.6 1.0
ND1 A:HIS226 4.4 63.8 1.0
CG A:HIS226 4.4 64.1 1.0
CA A:CYS210 4.6 54.2 1.0
C A:CYS213 4.7 57.2 1.0
N A:LEU214 4.8 56.3 1.0
CB A:LYS215 4.9 45.6 1.0
CA A:CYS230 4.9 0.2 1.0
C A:TYR212 4.9 55.9 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

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