Zinc in PDB 5b77: Crystal Structrue of Moz Double Phd Finger in Complex with Histone H3 Propionylation at K14

All present enzymatic activity of Crystal Structrue of Moz Double Phd Finger in Complex with Histone H3 Propionylation at K14:
2.3.1.48;

The structure of Crystal Structrue of Moz Double Phd Finger in Complex with Histone H3 Propionylation at K14, PDB code: 5b77 was solved by H.Li, X.Xiong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.80 / 1.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.708, 48.028, 75.168, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 20.4

The binding sites of Zinc atom in the Crystal Structrue of Moz Double Phd Finger in Complex with Histone H3 Propionylation at K14 (pdb code 5b77). 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 Structrue of Moz Double Phd Finger in Complex with Histone H3 Propionylation at K14, PDB code: 5b77:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structrue of Moz Double Phd Finger in Complex with Histone H3 Propionylation at K14


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structrue of Moz Double Phd Finger in Complex with Histone H3 Propionylation at K14 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:21.6 occ:1.00 SG A:CYS310 2.3 24.9 1.0 SG A:CYS284 2.3 21.2 1.0 SG A:CYS281 2.3 21.1 1.0 SG A:CYS307 2.3 23.3 1.0 CB A:CYS281 3.2 22.3 1.0 CB A:CYS284 3.3 23.1 1.0 CB A:CYS307 3.4 24.6 1.0 CB A:CYS310 3.5 22.8 1.0 N A:CYS284 3.7 21.2 1.0 N A:CYS307 4.0 23.8 1.0 N A:CYS310 4.0 27.5 1.0 CA A:CYS284 4.1 22.8 1.0 CA A:CYS307 4.2 24.5 1.0 CB A:SER283 4.3 26.7 1.0 CA A:CYS310 4.3 30.8 1.0 NH1 A:ARG286 4.5 27.8 1.0 OG A:SER283 4.6 29.4 1.0 C A:SER283 4.6 24.1 1.0 CA A:CYS281 4.6 18.4 1.0 C A:CYS307 4.7 26.6 1.0 O A:CYS307 4.8 26.1 1.0 C A:CYS284 4.8 20.5 1.0 CA A:SER283 4.8 22.9 1.0 N A:SER283 4.9 20.9 1.0 CB A:ILE309 4.9 35.5 1.0 N A:ASP285 5.0 17.4 1.0 C A:ILE309 5.0 32.8 1.0

Zinc binding site 2 out of 4 in the Crystal Structrue of Moz Double Phd Finger in Complex with Histone H3 Propionylation at K14


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structrue of Moz Double Phd Finger in Complex with Histone H3 Propionylation at K14 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:25.0 occ:1.00 ND1 A:HIS289 2.1 26.1 1.0 SG A:CYS292 2.3 26.2 1.0 SG A:CYS268 2.3 26.0 1.0 SG A:CYS265 2.3 20.6 1.0 CB A:CYS265 3.0 21.1 1.0 CE1 A:HIS289 3.0 24.0 1.0 CB A:CYS292 3.2 24.9 1.0 CG A:HIS289 3.2 22.7 1.0 CB A:CYS268 3.3 28.1 1.0 CB A:HIS289 3.6 22.2 1.0 N A:CYS268 3.8 24.5 1.0 O A:HOH629 4.0 39.5 1.0 N A:HIS289 4.1 18.4 1.0 CA A:CYS268 4.1 26.6 1.0 NE2 A:HIS289 4.2 23.2 1.0 CD2 A:HIS289 4.3 23.5 1.0 CA A:HIS289 4.4 19.5 1.0 CA A:CYS265 4.5 17.3 1.0 CA A:CYS292 4.6 28.0 1.0 CB A:SER267 4.8 29.2 1.0 C A:CYS268 4.9 28.7 1.0 C A:SER267 4.9 32.3 1.0 N A:CYS292 5.0 24.3 1.0

Zinc binding site 3 out of 4 in the Crystal Structrue of Moz Double Phd Finger in Complex with Histone H3 Propionylation at K14


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structrue of Moz Double Phd Finger in Complex with Histone H3 Propionylation at K14 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn403 b:19.4 occ:1.00 ND1 A:HIS238 2.1 16.9 1.0 SG A:CYS241 2.3 21.2 1.0 SG A:CYS212 2.3 19.6 1.0 SG A:CYS209 2.3 17.7 1.0 CE1 A:HIS238 3.0 21.0 1.0 CB A:CYS209 3.1 19.5 1.0 CG A:HIS238 3.2 20.2 1.0 CB A:CYS212 3.4 18.8 1.0 CB A:CYS241 3.4 19.1 1.0 CB A:HIS238 3.6 17.2 1.0 N A:CYS212 3.7 16.2 1.0 N A:HIS238 4.1 15.7 1.0 CA A:CYS212 4.1 20.8 1.0 NE2 A:HIS238 4.1 20.3 1.0 CD2 A:HIS238 4.3 22.1 1.0 O A:HOH512 4.4 25.2 1.0 CA A:HIS238 4.5 20.6 1.0 CA A:CYS209 4.6 17.8 1.0 CB A:PHE211 4.7 16.7 1.0 CA A:CYS241 4.7 17.8 1.0 C A:PHE211 4.8 18.3 1.0 C A:CYS212 4.8 19.6 1.0 CA A:ASN219 4.9 23.9 1.0 N A:CYS241 4.9 18.9 1.0 CG A:ARG220 4.9 23.4 1.0 N A:LEU213 5.0 17.7 1.0

Zinc binding site 4 out of 4 in the Crystal Structrue of Moz Double Phd Finger in Complex with Histone H3 Propionylation at K14


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structrue of Moz Double Phd Finger in Complex with Histone H3 Propionylation at K14 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn404 b:18.1 occ:1.00 SG A:CYS233 2.3 18.7 1.0 SG A:CYS262 2.3 18.2 1.0 SG A:CYS259 2.3 16.6 1.0 SG A:CYS230 2.3 16.6 1.0 CB A:CYS230 3.2 15.5 1.0 CB A:CYS262 3.2 16.8 1.0 CB A:CYS233 3.3 18.6 1.0 CB A:CYS259 3.4 14.9 1.0 N A:CYS233 3.7 17.1 1.0 N A:CYS259 4.0 15.3 1.0 CA A:CYS233 4.0 15.9 1.0 N A:CYS262 4.2 17.6 1.0 CA A:CYS259 4.3 14.8 1.0 CA A:CYS262 4.3 17.6 1.0 O B:HOH231 4.3 26.1 1.0 O A:HOH630 4.4 66.8 1.0 CA A:CYS230 4.6 15.5 1.0 C A:ASP232 4.7 19.5 1.0 CB A:ASP232 4.8 20.6 1.0 C A:CYS233 4.8 17.6 1.0 C A:CYS259 4.9 15.8 1.0 N A:GLY234 4.9 17.6 1.0

X.Xiong, T.Panchenko, S.Yang, S.Zhao, P.Yan, W.Zhang, W.Xie, Y.Li, Y.Zhao, C.D.Allis, H.Li. Selective Recognition of Histone Crotonylation By Double Phd Fingers of Moz and DPF2 Nat.Chem.Biol. V. 12 1111 2016.
ISSN: ESSN 1552-4469
PubMed: 27775714
DOI: 10.1038/NCHEMBIO.2218