Zinc in PDB 3qah: Crystal Structure of Apo-Form Human Mof Catalytic Domain

All present enzymatic activity of Crystal Structure of Apo-Form Human Mof Catalytic Domain:
2.3.1.48;

The structure of Crystal Structure of Apo-Form Human Mof Catalytic Domain, PDB code: 3qah was solved by B.Sun, Q.Tang, C.Zhong, J.Ding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.07 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.913, 60.690, 124.368, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 22.8

The binding sites of Zinc atom in the Crystal Structure of Apo-Form Human Mof Catalytic Domain (pdb code 3qah). 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 Crystal Structure of Apo-Form Human Mof Catalytic Domain, PDB code: 3qah:

Zinc binding site 1 out of 1 in the Crystal Structure of Apo-Form Human Mof Catalytic Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Apo-Form Human Mof Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:15.7 occ:1.00 NE2 A:HIS226 2.1 14.6 1.0 SG A:CYS213 2.3 13.0 1.0 SG A:CYS210 2.4 13.0 1.0 SG A:CYS230 2.4 16.8 1.0 CE1 A:HIS226 3.0 18.2 1.0 CB A:CYS210 3.1 13.3 1.0 CD2 A:HIS226 3.1 16.9 1.0 CB A:CYS230 3.2 21.7 1.0 CB A:CYS213 3.4 15.7 1.0 N A:CYS213 3.9 15.7 1.0 O A:HOH143 3.9 31.4 1.0 O A:HOH465 4.0 30.6 1.0 ND1 A:HIS226 4.1 19.8 1.0 CA A:CYS213 4.1 14.8 1.0 CG A:HIS226 4.2 17.8 1.0 CA A:CYS210 4.6 13.3 1.0 CA A:CYS230 4.6 22.4 1.0 C A:CYS213 4.8 14.0 1.0 CB A:LYS215 4.8 14.1 1.0 N A:LEU214 4.9 13.2 1.0 C A:TYR212 5.0 15.3 1.0

B.Sun, S.Guo, Q.Tang, C.Li, R.Zeng, Z.Xiong, C.Zhong, J.Ding. Regulation of the Histone Acetyltransferase Activity of Hmof Via Autoacetylation of LYS274 Cell Res. V. 21 1262 2011.
ISSN: ISSN 1001-0602
PubMed: 21691301
DOI: 10.1038/CR.2011.105