Zinc in PDB 3lqh: Crystal Structure of MLL1 PHD3-Bromo in the Free Form

All present enzymatic activity of Crystal Structure of MLL1 PHD3-Bromo in the Free Form:
2.1.1.43;

The structure of Crystal Structure of MLL1 PHD3-Bromo in the Free Form, PDB code: 3lqh was solved by Z.Wang, D.J.Patel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.72
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	63.219, 71.879, 93.867, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 23.4

The binding sites of Zinc atom in the Crystal Structure of MLL1 PHD3-Bromo in the Free Form (pdb code 3lqh). 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 MLL1 PHD3-Bromo in the Free Form, PDB code: 3lqh:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of MLL1 PHD3-Bromo in the Free Form


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 MLL1 PHD3-Bromo in the Free Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1001 b:18.0 occ:1.00 ND1 A:HIS1596 2.3 23.3 1.0 SG A:CYS1572 2.3 17.9 1.0 SG A:CYS1599 2.3 18.2 1.0 SG A:CYS1569 2.4 13.8 1.0 CB A:CYS1569 3.1 15.0 1.0 CE1 A:HIS1596 3.1 14.2 1.0 CB A:CYS1572 3.2 16.8 1.0 CG A:HIS1596 3.3 14.9 1.0 CB A:CYS1599 3.3 12.9 1.0 CB A:HIS1596 3.5 14.2 1.0 N A:CYS1572 3.8 17.1 1.0 N A:HIS1596 4.1 9.9 1.0 CA A:CYS1572 4.1 17.9 1.0 NE2 A:HIS1596 4.2 20.0 1.0 O A:HOH135 4.3 33.2 1.0 C A:LEU1571 4.3 19.6 1.0 CA A:HIS1596 4.3 11.5 1.0 CD2 A:HIS1596 4.3 16.3 1.0 CA A:CYS1569 4.5 12.4 1.0 CB A:LEU1571 4.7 20.0 1.0 CA A:CYS1599 4.7 22.2 1.0 O A:LEU1571 4.7 19.6 1.0 N A:LEU1571 4.8 19.4 1.0 CA A:LEU1571 4.8 17.2 1.0 O A:CYS1569 4.8 14.1 1.0 C A:CYS1569 4.8 13.9 1.0 C A:CYS1572 5.0 18.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of MLL1 PHD3-Bromo in the Free Form


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 MLL1 PHD3-Bromo in the Free Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1002 b:13.6 occ:1.00 SG A:CYS1591 2.4 13.9 1.0 SG A:CYS1621 2.4 13.3 1.0 SG A:CYS1624 2.4 14.6 1.0 SG A:CYS1588 2.4 10.3 1.0 CB A:CYS1588 3.2 10.5 1.0 CB A:CYS1624 3.3 15.0 1.0 CB A:CYS1591 3.3 14.6 1.0 CB A:CYS1621 3.5 10.1 1.0 N A:CYS1591 3.8 11.9 1.0 N A:CYS1621 3.9 11.2 1.0 CA A:CYS1591 4.1 11.7 1.0 N A:CYS1624 4.2 15.8 1.0 CA A:CYS1621 4.2 10.2 1.0 CA A:CYS1624 4.3 16.4 1.0 CA A:CYS1588 4.7 11.3 1.0 CB A:LYS1590 4.7 29.8 1.0 C A:CYS1621 4.7 11.6 1.0 O A:CYS1621 4.7 12.7 1.0 C A:LYS1590 4.8 18.5 1.0 C A:ASN1623 4.9 22.4 1.0 C A:CYS1591 4.9 10.3 1.0 CB A:ASN1623 5.0 23.5 1.0

Z.Wang, J.Song, T.A.Milne, G.G.Wang, H.Li, C.D.Allis, D.J.Patel. Pro Isomerization in MLL1 PHD3-Bromo Cassette Connects H3K4ME Readout to CYP33 and Hdac-Mediated Repression. Cell(Cambridge,Mass.) V. 141 1183 2010.
ISSN: ISSN 0092-8674
PubMed: 20541251
DOI: 10.1016/J.CELL.2010.05.016