Zinc in PDB 7lbq: Crystal Structure of Human Survivin Bound to Histone H3 T3PHK4ME2 Peptide

The structure of Crystal Structure of Human Survivin Bound to Histone H3 T3PHK4ME2 Peptide, PDB code: 7lbq was solved by E.Niedzialkowska, W.Minor, P.T.Stukenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.36 / 2.69
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	69.343, 70.162, 89.447, 90, 90, 90
R / Rfree (%)	24.9 / 26.8

The binding sites of Zinc atom in the Crystal Structure of Human Survivin Bound to Histone H3 T3PHK4ME2 Peptide (pdb code 7lbq). 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 Human Survivin Bound to Histone H3 T3PHK4ME2 Peptide, PDB code: 7lbq:

Zinc binding site 1 out of 1 in the Crystal Structure of Human Survivin Bound to Histone H3 T3PHK4ME2 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 Human Survivin Bound to Histone H3 T3PHK4ME2 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:25.9 occ:1.00 NE2 A:HIS77 2.0 43.1 1.0 SG A:CYS57 2.3 22.9 1.0 SG A:CYS84 2.3 34.5 1.0 SG A:CYS60 2.4 31.9 1.0 CE1 A:HIS77 2.7 41.4 1.0 CB A:CYS84 3.0 39.0 1.0 CB A:CYS57 3.1 24.9 1.0 CB A:CYS60 3.2 32.3 1.0 CD2 A:HIS77 3.3 45.1 1.0 N A:CYS60 3.7 28.1 1.0 ND1 A:HIS77 3.9 42.0 1.0 CA A:CYS60 4.0 31.7 1.0 CG A:HIS77 4.2 43.7 1.0 CA A:CYS84 4.5 42.5 1.0 CA A:CYS57 4.6 25.2 1.0 OG A:SER81 4.6 52.6 1.0 C A:PHE59 4.7 28.0 1.0 CB A:PHE59 4.7 23.9 1.0 C A:CYS60 4.8 34.2 1.0 CB A:SER81 4.9 51.4 1.0 N A:PHE61 4.9 33.0 1.0 CB A:PHE86 4.9 26.0 1.0 N A:PHE59 4.9 26.0 1.0

E.Niedzialkowska, L.Liu, C.Kuscu, Z.Mayo, W.Minor, B.D.Strahl, M.Adli, P.T.Stukenberg. TIP60 Acetylation of Histone H3K4 Temporally Controls Chromosome Passenger Complex Localization. Mol.Biol.Cell V. 33 BR15 2022.
ISSN: ESSN 1939-4586
PubMed: 35653296
DOI: 10.1091/MBC.E21-06-0283