Zinc in PDB 5jle: Crystal Structure of SETD2 Bound to Sah

All present enzymatic activity of Crystal Structure of SETD2 Bound to Sah:
2.1.1.43;

The structure of Crystal Structure of SETD2 Bound to Sah, PDB code: 5jle was solved by H.Li, S.Yang, X.Zheng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.88 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.540, 77.152, 78.693, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 25

The binding sites of Zinc atom in the Crystal Structure of SETD2 Bound to Sah (pdb code 5jle). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of SETD2 Bound to Sah, PDB code: 5jle:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Crystal Structure of SETD2 Bound to Sah


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 SETD2 Bound to Sah within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1801 b:69.4 occ:1.00 SG A:CYS1499 2.3 60.9 1.0 SG A:CYS1501 2.3 75.6 1.0 SG A:CYS1520 2.6 63.4 1.0 SG A:CYS1516 2.6 61.7 1.0 CB A:CYS1501 3.1 72.9 1.0 CB A:CYS1520 3.3 68.8 1.0 CB A:CYS1499 3.4 78.1 1.0 CB A:CYS1516 3.4 68.6 1.0 ZN A:ZN1802 3.8 63.3 1.0 CA A:CYS1516 3.9 70.8 1.0 N A:CYS1501 4.0 81.0 1.0 CA A:CYS1520 4.1 72.3 1.0 CA A:CYS1501 4.2 80.4 1.0 SG A:CYS1529 4.3 63.1 1.0 N A:LEU1521 4.7 73.2 1.0 SG A:CYS1533 4.8 68.8 1.0 CA A:CYS1499 4.8 77.1 1.0 N A:CYS1516 4.8 66.7 1.0 C A:CYS1520 4.8 73.3 1.0 N A:GLU1500 4.8 75.2 1.0 C A:CYS1516 5.0 73.6 1.0

Zinc binding site 2 out of 3 in the Crystal Structure of SETD2 Bound to Sah


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 SETD2 Bound to Sah within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1802 b:63.3 occ:1.00 SG A:CYS1516 2.3 61.7 1.0 SG A:CYS1539 2.3 58.2 1.0 SG A:CYS1529 2.3 63.1 1.0 SG A:CYS1533 2.4 68.8 1.0 CB A:CYS1529 3.1 62.8 1.0 CB A:CYS1516 3.5 68.6 1.0 CB A:CYS1533 3.5 65.7 1.0 CB A:CYS1539 3.5 61.9 1.0 ZN A:ZN1801 3.8 69.4 1.0 SG A:CYS1499 4.2 60.9 1.0 O A:HOH1930 4.4 60.9 1.0 CB A:ASN1541 4.5 63.0 1.0 CA A:CYS1539 4.5 64.1 1.0 CA A:CYS1529 4.6 64.0 1.0 CA A:CYS1533 4.8 68.0 1.0 SG A:CYS1520 4.8 63.4 1.0 CA A:CYS1516 4.9 70.8 1.0

Zinc binding site 3 out of 3 in the Crystal Structure of SETD2 Bound to Sah


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 SETD2 Bound to Sah within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1803 b:70.5 occ:1.00 SG A:CYS1678 2.2 69.9 1.0 SG A:CYS1680 2.3 69.0 1.0 SG A:CYS1631 2.4 68.3 1.0 SG A:CYS1685 2.6 80.1 1.0 CB A:CYS1685 3.1 79.9 1.0 CB A:CYS1680 3.3 69.8 1.0 CB A:CYS1631 3.4 75.3 1.0 CB A:CYS1678 3.5 70.0 1.0 CA A:CYS1685 3.7 81.0 1.0 N A:CYS1631 3.8 70.2 1.0 N A:CYS1680 4.1 71.7 1.0 N A:ARG1686 4.1 82.8 1.0 NE2 A:HIS1629 4.2 68.2 1.0 CA A:CYS1680 4.3 71.9 1.0 CA A:CYS1631 4.3 69.7 1.0 C A:CYS1685 4.3 79.2 1.0 CD2 A:HIS1629 4.4 67.2 1.0 O A:CYS1678 4.6 68.0 1.0 C A:CYS1678 4.7 71.0 1.0 CA A:CYS1678 4.7 70.4 1.0 N A:GLY1687 4.7 78.4 1.0 C A:SER1630 4.8 71.2 1.0 N A:GLY1681 4.8 73.2 1.0 C A:CYS1680 4.9 71.2 1.0 N A:CYS1685 4.9 84.0 1.0

S.Yang, X.Zheng, C.Lu, G.M.Li, C.D.Allis, H.Li. Molecular Basis For Oncohistone H3 Recognition By SETD2 Methyltransferase Genes Dev. V. 30 1611 2016.
ISSN: ISSN 0890-9369
PubMed: 27474439
DOI: 10.1101/GAD.284323.116