Zinc in PDB 2pnx: The Phd Finger of ING4 in Complex with An H3K4ME3 Histone Peptide

The structure of The Phd Finger of ING4 in Complex with An H3K4ME3 Histone Peptide, PDB code: 2pnx was solved by K.S.Champagne, K.Johnson, T.G.Kutateladze, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.08 / 1.80
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	68.160, 68.160, 27.960, 90.00, 90.00, 90.00
R / Rfree (%)	19.9 / 21.1

The binding sites of Zinc atom in the The Phd Finger of ING4 in Complex with An H3K4ME3 Histone Peptide (pdb code 2pnx). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the The Phd Finger of ING4 in Complex with An H3K4ME3 Histone Peptide, PDB code: 2pnx:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the The Phd Finger of ING4 in Complex with An H3K4ME3 Histone Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Phd Finger of ING4 in Complex with An H3K4ME3 Histone Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:18.3 occ:1.00 CD2 A:HIS223 2.2 8.6 1.0 SG A:CYS226 2.3 10.3 1.0 SG A:CYS201 2.3 8.3 1.0 SG A:CYS199 2.3 12.0 1.0 CB A:CYS199 3.0 10.5 1.0 CG A:HIS223 3.1 10.6 1.0 CB A:CYS226 3.1 9.6 1.0 NE2 A:HIS223 3.3 11.1 1.0 CB A:CYS201 3.4 9.1 1.0 CB A:HIS223 3.5 9.6 1.0 N A:CYS201 4.0 9.5 1.0 N A:HIS223 4.1 9.8 1.0 O A:HOH410 4.1 10.2 1.0 ND1 A:HIS223 4.3 12.3 1.0 CA A:CYS201 4.3 8.6 1.0 CE1 A:HIS223 4.3 7.1 1.0 CA A:HIS223 4.4 9.2 1.0 CA A:CYS199 4.4 10.2 1.0 O A:HOH407 4.5 12.3 1.0 N A:LEU200 4.5 8.9 1.0 CA A:CYS226 4.6 9.9 1.0 OH A:TYR206 4.6 13.7 1.0 C A:CYS199 4.8 10.4 1.0 O A:HIS223 4.9 9.0 1.0

Zinc binding site 2 out of 4 in the The Phd Finger of ING4 in Complex with An H3K4ME3 Histone Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Phd Finger of ING4 in Complex with An H3K4ME3 Histone Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:17.1 occ:1.00 SG A:CYS239 2.3 9.9 1.0 SG A:CYS212 2.3 8.6 1.0 SG A:CYS242 2.4 9.8 1.0 SG A:CYS217 2.4 9.7 1.0 CB A:CYS212 3.2 9.9 1.0 CB A:CYS217 3.2 9.6 1.0 CB A:CYS242 3.3 11.2 1.0 CB A:CYS239 3.4 9.7 1.0 N A:CYS239 4.0 9.9 1.0 CA A:CYS217 4.1 10.2 1.0 N A:CYS242 4.1 11.3 1.0 CA A:CYS239 4.2 10.5 1.0 CA A:CYS242 4.3 12.6 1.0 CZ A:PHE222 4.3 10.6 1.0 CE1 A:PHE222 4.5 10.3 1.0 CB A:ASN214 4.6 9.8 1.0 CA A:CYS212 4.6 9.0 1.0 C A:CYS239 4.8 10.5 1.0 O A:CYS239 4.8 9.6 1.0 ND2 A:ASN214 4.9 9.6 1.0

Zinc binding site 3 out of 4 in the The Phd Finger of ING4 in Complex with An H3K4ME3 Histone Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of The Phd Finger of ING4 in Complex with An H3K4ME3 Histone Peptide within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn300 b:22.6 occ:1.00 ND1 C:HIS223 2.2 13.2 1.0 SG C:CYS226 2.3 11.8 1.0 SG C:CYS201 2.3 12.2 1.0 SG C:CYS199 2.3 12.0 1.0 CB C:CYS199 3.0 13.1 1.0 CB C:CYS226 3.2 13.2 1.0 CE1 C:HIS223 3.2 13.9 1.0 CG C:HIS223 3.2 13.4 1.0 CB C:CYS201 3.4 15.6 1.0 CB C:HIS223 3.5 13.6 1.0 O C:HOH412 3.9 18.2 1.0 N C:CYS201 4.0 14.9 1.0 N C:HIS223 4.0 12.3 1.0 CA C:CYS201 4.3 14.6 1.0 NE2 C:HIS223 4.3 12.3 1.0 CD2 C:HIS223 4.4 13.0 1.0 CA C:HIS223 4.4 12.6 1.0 CA C:CYS199 4.4 13.3 1.0 N C:LEU200 4.5 14.8 1.0 OH C:TYR206 4.6 17.3 1.0 O C:HOH415 4.6 22.4 1.0 CA C:CYS226 4.6 13.7 1.0 C C:CYS199 4.8 14.2 1.0 O C:HIS223 4.9 11.5 1.0 O C:TYR198 4.9 13.0 1.0

Zinc binding site 4 out of 4 in the The Phd Finger of ING4 in Complex with An H3K4ME3 Histone Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of The Phd Finger of ING4 in Complex with An H3K4ME3 Histone Peptide within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn400 b:24.2 occ:1.00 SG C:CYS239 2.3 16.1 1.0 SG C:CYS212 2.3 13.7 1.0 SG C:CYS242 2.3 17.8 1.0 SG C:CYS217 2.4 15.0 1.0 CB C:CYS212 3.1 13.2 1.0 CB C:CYS217 3.2 16.3 1.0 CB C:CYS242 3.3 21.4 1.0 CB C:CYS239 3.4 15.8 1.0 N C:CYS239 4.0 15.3 1.0 N C:CYS242 4.1 23.2 1.0 CA C:CYS217 4.1 18.2 1.0 CA C:CYS239 4.2 16.9 1.0 CA C:CYS242 4.3 23.6 1.0 O C:HOH436 4.3 34.3 1.0 CZ C:PHE222 4.4 14.8 1.0 CB C:ASN214 4.5 14.4 1.0 CE1 C:PHE222 4.6 14.8 1.0 CA C:CYS212 4.6 13.5 1.0 ND2 C:ASN214 4.7 14.7 1.0 C C:CYS239 4.8 18.2 1.0 O C:CYS239 4.8 17.5 1.0

T.Hung, O.Binda, K.S.Champagne, A.J.Kuo, K.Johnson, H.Y.Chang, M.D.Simon, T.G.Kutateladze, O.Gozani. ING4 Mediates Crosstalk Between Histone H3 K4 Trimethylation and H3 Acetylation to Attenuate Cellular Transformation Mol.Cell V. 33 248 2009.
ISSN: ISSN 1097-2765
PubMed: 19187765
DOI: 10.1016/J.MOLCEL.2008.12.016