Zinc in PDB 5wci: Human Myst Histone Acetyltransferase 1

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

The structure of Human Myst Histone Acetyltransferase 1, PDB code: 5wci was solved by A.Dong, H.Zeng, J.R.Walker, C.Bountra, C.H.Arrowsmith, A.M.Edwards, Y.G.Zheng, P.J.Brown, H.Wu, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.78
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.336, 58.729, 120.277, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 21.8

The structure of Human Myst Histone Acetyltransferase 1 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Human Myst Histone Acetyltransferase 1 (pdb code 5wci). 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 Myst Histone Acetyltransferase 1, PDB code: 5wci:

Zinc binding site 1 out of 1 in the Human 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 Human Myst Histone Acetyltransferase 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:16.0 occ:1.00 NE2 A:HIS226 2.1 14.8 1.0 SG A:CYS213 2.3 14.3 1.0 SG A:CYS210 2.3 12.2 1.0 SG A:CYS230 2.3 16.0 1.0 CD2 A:HIS226 3.0 14.6 1.0 CE1 A:HIS226 3.1 16.2 1.0 CB A:CYS210 3.1 12.5 1.0 CB A:CYS230 3.2 18.1 1.0 CB A:CYS213 3.3 14.3 1.0 O A:HOH749 3.8 26.8 1.0 N A:CYS213 3.9 13.6 1.0 O A:HOH814 4.1 34.7 1.0 CA A:CYS213 4.1 13.8 1.0 CG A:HIS226 4.2 14.8 1.0 ND1 A:HIS226 4.2 14.9 1.0 CA A:CYS210 4.6 12.7 1.0 CA A:CYS230 4.6 18.1 1.0 O A:HOH820 4.6 22.1 1.0 C A:CYS213 4.8 13.7 1.0 CB A:LYS215 4.9 16.9 1.0 CB A:TRP232 5.0 17.6 0.5

H.Zeng, A.Dong, J.R.Walker, C.Bountra, C.H.Arrowsmith, A.M.Edwards, Y.G.Zheng, P.J.Brown, H.Wu, Structural Genomics Consortium (Sgc). Human Myst Histone Acetyltransferase 1 To Be Published.