Zinc in PDB 4lk9: Crystal Structure of Moz Double Phd Finger Histone H3 Tail Complex

All present enzymatic activity of Crystal Structure of Moz Double Phd Finger Histone H3 Tail Complex:
2.3.1.48;

The structure of Crystal Structure of Moz Double Phd Finger Histone H3 Tail Complex, PDB code: 4lk9 was solved by I.Dreveny, S.E.Deeves, B.Yue, D.M.Heery, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.86 / 1.60
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	70.519, 70.519, 96.827, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 18.6

The binding sites of Zinc atom in the Crystal Structure of Moz Double Phd Finger Histone H3 Tail Complex (pdb code 4lk9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Moz Double Phd Finger Histone H3 Tail Complex, PDB code: 4lk9:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of Moz Double Phd Finger Histone H3 Tail Complex


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 Moz Double Phd Finger Histone H3 Tail Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:14.5 occ:1.00 SG A:CYS284 2.3 13.7 1.0 SG A:CYS307 2.3 16.1 1.0 SG A:CYS310 2.4 16.2 1.0 SG A:CYS281 2.4 14.0 1.0 CB A:CYS281 3.2 13.4 1.0 CB A:CYS284 3.3 14.5 1.0 CB A:CYS310 3.4 16.7 1.0 CB A:CYS307 3.5 14.5 1.0 N A:CYS284 3.8 13.3 1.0 N A:CYS307 3.9 16.0 1.0 N A:CYS310 4.1 19.0 1.0 CA A:CYS284 4.1 11.5 1.0 CA A:CYS307 4.2 16.0 1.0 CB A:SER283 4.3 14.0 1.0 CA A:CYS310 4.4 18.2 1.0 OG A:SER283 4.4 18.5 1.0 NH1 A:ARG286 4.5 15.8 1.0 C A:SER283 4.5 14.7 1.0 O A:CYS307 4.6 18.1 1.0 C A:CYS307 4.7 21.3 1.0 CA A:CYS281 4.7 12.0 1.0 CA A:SER283 4.8 13.9 1.0 C A:CYS284 4.9 15.0 1.0 CB A:ILE309 4.9 18.7 1.0 N A:SER283 4.9 13.3 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of Moz Double Phd Finger Histone H3 Tail Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Moz Double Phd Finger Histone H3 Tail Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:22.7 occ:1.00 ND1 A:HIS289 2.1 26.6 1.0 SG A:CYS292 2.3 25.8 1.0 SG A:CYS268 2.3 28.2 1.0 SG A:CYS265 2.4 22.2 1.0 CE1 A:HIS289 3.0 25.3 1.0 CB A:CYS265 3.0 21.3 1.0 CG A:HIS289 3.1 21.0 1.0 CB A:CYS268 3.3 30.2 1.0 CB A:CYS292 3.3 24.4 1.0 CB A:HIS289 3.5 19.8 1.0 N A:CYS268 3.7 26.4 1.0 CA A:CYS268 4.1 29.1 1.0 NE2 A:HIS289 4.1 25.7 1.0 N A:HIS289 4.2 16.9 1.0 CD2 A:HIS289 4.2 24.8 1.0 CA A:HIS289 4.5 19.6 1.0 CA A:CYS265 4.5 19.0 1.0 O A:HOH647 4.6 41.2 1.0 CA A:CYS292 4.7 24.6 1.0 CB A:SER267 4.8 25.0 1.0 C A:SER267 4.8 28.1 1.0 C A:CYS268 4.9 30.3 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of Moz Double Phd Finger Histone H3 Tail Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Moz Double Phd Finger Histone H3 Tail Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:13.5 occ:1.00 ND1 A:HIS238 2.1 14.4 1.0 SG A:CYS241 2.3 16.0 1.0 SG A:CYS212 2.3 14.5 1.0 SG A:CYS209 2.4 12.3 1.0 CE1 A:HIS238 3.0 15.5 1.0 CB A:CYS209 3.1 14.1 1.0 CG A:HIS238 3.2 14.2 1.0 CB A:CYS212 3.3 16.4 1.0 CB A:CYS241 3.4 13.9 1.0 CB A:HIS238 3.6 12.9 1.0 N A:CYS212 3.8 11.7 1.0 N A:HIS238 4.1 12.3 1.0 CA A:CYS212 4.1 12.5 1.0 NE2 A:HIS238 4.2 15.8 1.0 CD2 A:HIS238 4.3 14.7 1.0 O A:HOH528 4.5 22.4 1.0 CA A:HIS238 4.5 12.9 1.0 CB A:PHE211 4.5 12.5 1.0 CA A:CYS209 4.6 14.4 1.0 CA A:CYS241 4.7 12.7 1.0 C A:PHE211 4.8 15.6 1.0 CA A:ASN219 4.8 19.2 1.0 C A:CYS212 4.9 14.4 1.0 CG A:ARG220 4.9 28.5 1.0 N A:ARG220 4.9 23.3 1.0 N A:CYS241 5.0 12.7 1.0 N A:LEU213 5.0 13.9 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of Moz Double Phd Finger Histone H3 Tail Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Moz Double Phd Finger Histone H3 Tail Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn404 b:14.6 occ:1.00 SG A:CYS233 2.3 15.3 1.0 SG A:CYS262 2.3 17.9 1.0 SG A:CYS259 2.3 14.9 1.0 SG A:CYS230 2.4 13.9 1.0 CB A:CYS262 3.2 14.4 1.0 CB A:CYS230 3.3 11.7 1.0 CB A:CYS233 3.3 19.1 1.0 CB A:CYS259 3.5 12.0 1.0 N A:CYS233 3.7 16.6 1.0 N A:CYS259 4.0 10.3 1.0 CA A:CYS233 4.1 17.6 1.0 O A:HOH582 4.2 33.6 1.0 N A:CYS262 4.2 16.6 1.0 CA A:CYS262 4.3 17.4 1.0 CA A:CYS259 4.3 11.3 1.0 O A:HOH598 4.5 37.3 1.0 CB A:ASP232 4.6 16.9 1.0 O A:HOH554 4.7 24.8 1.0 CB A:ASN235 4.7 14.8 1.0 CA A:CYS230 4.7 11.4 1.0 C A:CYS233 4.8 17.6 1.0 C A:ASP232 4.8 19.1 1.0 N A:GLY234 4.8 15.9 1.0 N A:ASN235 4.9 14.2 1.0 C A:CYS259 4.9 15.2 1.0

I.Dreveny, S.E.Deeves, J.Fulton, B.Yue, M.Messmer, A.Bhattacharya, H.M.Collins, D.M.Heery. The Double Phd Finger Domain of Moz/MYST3 Induces Alpha-Helical Structure of the Histone H3 Tail to Facilitate Acetylation and Methylation Sampling and Modification. Nucleic Acids Res. V. 42 822 2014.
ISSN: ISSN 0305-1048
PubMed: 24150941
DOI: 10.1093/NAR/GKT931