Zinc in PDB 2giv: 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: 2giv was solved by J.Min, H.Wu, P.Loppnau, J.Weigelt, M.Sundstrom, C.H.Arrowsmith, A.M.Edwards, A.Bochkarev, A.N.Plotnikov, Structural Genomicsconsortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.89 / 1.94
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.305, 58.577, 119.753, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 26.2

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 2giv). 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: 2giv:

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:25.3 occ:1.00 NE2 A:HIS53 2.2 24.7 1.0 SG A:CYS40 2.2 23.2 1.0 SG A:CYS57 2.3 25.1 1.0 SG A:CYS37 2.4 20.8 1.0 CE1 A:HIS53 3.0 25.5 1.0 CB A:CYS37 3.2 21.6 1.0 CB A:CYS40 3.2 23.1 1.0 CB A:CYS57 3.2 26.1 1.0 CD2 A:HIS53 3.2 23.4 1.0 N A:CYS40 3.9 22.1 1.0 O A:HOH553 4.0 38.7 1.0 CA A:CYS40 4.1 22.9 1.0 O A:HOH610 4.1 48.0 1.0 ND1 A:HIS53 4.2 27.0 1.0 O A:HOH667 4.2 44.7 1.0 CG A:HIS53 4.3 24.3 1.0 O A:HOH662 4.5 39.2 1.0 CA A:CYS57 4.6 27.0 1.0 CA A:CYS37 4.7 22.2 1.0 CB A:LYS42 4.8 24.2 1.0 C A:CYS40 4.8 23.3 1.0 N A:LEU41 5.0 22.8 1.0

H.Wu, J.Min, P.Loppnau, J.Weigelt, M.Sundstrom, C.H.Arrowsmith, A.M.Edwards, A.Bochkarev, A.N.Plotnikov. The Crystal Structure of Human Myst Histone Acetyltransferase 1 in Complex with Acetylcoenzyme A To Be Published.