Zinc in PDB 2qic: Crystal Structure of the ING1 Phd Finger in Complex with A Histone H3K4ME3 Peptide

The structure of Crystal Structure of the ING1 Phd Finger in Complex with A Histone H3K4ME3 Peptide, PDB code: 2qic was solved by P.V.Pena, K.Champagne, R.Zhao, T.G.Kutateladze, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.10
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	49.060, 49.060, 52.620, 90.00, 90.00, 120.00
R / Rfree (%)	24 / 26.4

The binding sites of Zinc atom in the Crystal Structure of the ING1 Phd Finger in Complex with A Histone H3K4ME3 Peptide (pdb code 2qic). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the ING1 Phd Finger in Complex with A Histone H3K4ME3 Peptide, PDB code: 2qic:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the ING1 Phd Finger in Complex with A Histone H3K4ME3 Peptide


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 the ING1 Phd Finger in Complex with A Histone H3K4ME3 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:35.4 occ:1.00 ND1 A:HIS237 2.2 31.0 1.0 SG A:CYS240 2.3 39.4 1.0 SG A:CYS215 2.3 41.8 1.0 SG A:CYS213 2.4 36.5 1.0 CB A:CYS213 3.0 43.3 1.0 CE1 A:HIS237 3.1 28.5 1.0 CB A:CYS240 3.2 35.7 1.0 CG A:HIS237 3.2 30.8 1.0 CB A:CYS215 3.5 48.1 1.0 O A:HOH405 3.5 38.4 1.0 CB A:HIS237 3.6 30.0 1.0 N A:HIS237 4.0 31.0 1.0 N A:CYS215 4.2 47.9 1.0 NE2 A:HIS237 4.2 31.2 1.0 CD2 A:HIS237 4.3 31.9 1.0 OH A:TYR220 4.4 38.4 1.0 CA A:HIS237 4.4 30.7 1.0 CA A:CYS213 4.4 41.9 1.0 CA A:CYS215 4.4 48.0 1.0 CA A:CYS240 4.6 36.9 1.0 N A:LEU214 4.6 43.5 1.0 C A:CYS213 4.9 42.3 1.0 N A:CYS240 4.9 37.0 1.0 O A:HIS237 4.9 31.5 1.0 O A:TYR212 4.9 39.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the ING1 Phd Finger in Complex with A Histone H3K4ME3 Peptide


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 the ING1 Phd Finger in Complex with A Histone H3K4ME3 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:36.2 occ:1.00 SG A:CYS226 2.4 30.1 1.0 SG A:CYS253 2.4 32.1 1.0 SG A:CYS231 2.4 30.6 1.0 SG A:CYS256 2.4 31.1 1.0 CB A:CYS226 3.1 29.2 1.0 CB A:CYS231 3.1 31.3 1.0 CB A:CYS256 3.2 37.3 1.0 CB A:CYS253 3.4 33.2 1.0 N A:CYS253 3.9 35.9 1.0 CA A:CYS231 4.2 30.5 1.0 CA A:CYS253 4.2 35.6 1.0 N A:CYS256 4.4 39.8 1.0 CA A:CYS256 4.4 39.2 1.0 CA A:CYS226 4.6 27.8 1.0 CB A:ASN228 4.6 30.2 1.0 CE1 A:PHE236 4.7 31.5 1.0 CZ A:PHE236 4.8 31.3 1.0 C A:CYS253 4.9 38.3 1.0 O A:CYS253 4.9 37.7 1.0 ND2 A:ASN228 5.0 30.6 1.0

P.V.Pena, R.A.Hom, T.Hung, H.Lin, A.J.Kuo, R.P.Wong, O.M.Subach, K.S.Champagne, R.Zhao, V.V.Verkhusha, G.Li, O.Gozani, T.G.Kutateladze. Histone H3K4ME3 Binding Is Required For the Dna Repair and Apoptotic Activities of ING1 Tumor Suppressor. J.Mol.Biol. V. 380 303 2008.
ISSN: ISSN 0022-2836
PubMed: 18533182
DOI: 10.1016/J.JMB.2008.04.061