Zinc in PDB 2pq8: Myst Histone Acetyltransferase 1

All present enzymatic activity of Myst Histone Acetyltransferase 1:
2.3.1.48;

The structure of Myst Histone Acetyltransferase 1, PDB code: 2pq8 was solved by W.Tempel, H.Wu, L.Dombrovski, P.Loppnau, J.Weigelt, M.Sundstrom, C.H.Arrowsmith, A.M.Edwards, A.Bochkarev, A.N.Plotnikov, Structuralgenomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.060, 64.172, 93.383, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 23.1

The binding sites of Zinc atom in the Myst Histone Acetyltransferase 1 (pdb code 2pq8). 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 Myst Histone Acetyltransferase 1, PDB code: 2pq8:

Zinc binding site 1 out of 1 in the Myst Histone Acetyltransferase 1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Myst Histone Acetyltransferase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:11.4 occ:1.00 NE2 A:HIS226 2.1 11.5 1.0 SG A:CYS230 2.3 13.1 1.0 SG A:CYS210 2.3 10.6 1.0 SG A:CYS213 2.3 11.0 1.0 CD2 A:HIS226 3.0 10.1 1.0 CE1 A:HIS226 3.1 14.0 1.0 CB A:CYS210 3.2 10.2 1.0 CB A:CYS230 3.2 14.5 1.0 CB A:CYS213 3.3 12.3 1.0 N A:CYS213 3.9 9.6 1.0 ND1 A:HIS226 4.1 15.1 1.0 CG A:HIS226 4.2 12.9 1.0 O A:HOH89 4.2 27.4 1.0 CA A:CYS213 4.2 10.3 1.0 O A:HOH120 4.6 35.0 1.0 CA A:CYS230 4.6 15.4 1.0 CA A:CYS210 4.6 8.2 1.0 C A:CYS213 4.9 10.8 1.0 CB A:LYS215 4.9 10.7 1.0 N A:LEU214 5.0 9.3 1.0

H.Wu, W.Tempel, L.Dombrovski, P.Loppnau, J.Weigelt, M.Sundstrom, C.H.Arrowsmith, A.M.Edwards, A.Bochkarev, A.N.Plotnikov. Myst Histone Acetyltransferase 1. To Be Published.