Zinc in PDB 5f6l: The Crystal Structure of MLL1 (N3861I/Q3867L) in Complex with RBBP5 and ASH2L

All present enzymatic activity of The Crystal Structure of MLL1 (N3861I/Q3867L) in Complex with RBBP5 and ASH2L:
2.1.1.43;

The structure of The Crystal Structure of MLL1 (N3861I/Q3867L) in Complex with RBBP5 and ASH2L, PDB code: 5f6l was solved by Y.Li, M.Lei, Y.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.54 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	74.966, 44.410, 117.792, 90.00, 106.16, 90.00
R / Rfree (%)	16.6 / 21.3

The binding sites of Zinc atom in the The Crystal Structure of MLL1 (N3861I/Q3867L) in Complex with RBBP5 and ASH2L (pdb code 5f6l). 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 The Crystal Structure of MLL1 (N3861I/Q3867L) in Complex with RBBP5 and ASH2L, PDB code: 5f6l:

Zinc binding site 1 out of 1 in the The Crystal Structure of MLL1 (N3861I/Q3867L) in Complex with RBBP5 and ASH2L


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of MLL1 (N3861I/Q3867L) in Complex with RBBP5 and ASH2L within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn4002 b:25.5 occ:1.00 SG A:CYS3957 2.3 28.5 1.0 SG A:CYS3959 2.3 25.2 1.0 SG A:CYS3964 2.3 32.1 1.0 SG A:CYS3909 2.4 29.1 1.0 CB A:CYS3964 3.2 35.3 1.0 CB A:CYS3957 3.4 32.1 1.0 CB A:CYS3959 3.4 25.2 1.0 CB A:CYS3909 3.4 33.1 1.0 CA A:CYS3964 3.6 35.8 1.0 N A:ARG3965 3.9 36.1 1.0 N A:CYS3909 3.9 21.8 1.0 N A:CYS3959 4.0 27.4 1.0 C A:CYS3964 4.2 36.2 1.0 CA A:CYS3959 4.3 26.4 1.0 O A:HOH4184 4.3 26.7 1.0 CA A:CYS3909 4.3 27.7 1.0 N A:LYS3966 4.5 39.6 1.0 CA A:CYS3957 4.6 33.2 1.0 C A:CYS3957 4.6 34.9 1.0 NE2 A:HIS3907 4.7 28.2 1.0 CD2 A:HIS3907 4.7 25.5 1.0 N A:GLY3960 4.8 29.8 1.0 N A:ASN3958 4.8 30.7 1.0 N A:CYS3964 4.8 38.3 1.0 O A:CYS3957 4.9 36.5 1.0 C A:SER3908 4.9 20.6 1.0 C A:CYS3959 4.9 26.9 1.0

Y.Li, J.Han, Y.Zhang, F.Cao, Z.Liu, S.Li, J.Wu, C.Hu, Y.Wang, J.Shuai, J.Chen, L.Cao, D.Li, P.Shi, C.Tian, J.Zhang, Y.Dou, G.Li, Y.Chen, M.Lei. Structural Basis For Activity Regulation of Mll Family Methyltransferases. Nature V. 530 447 2016.
ISSN: ESSN 1476-4687
PubMed: 26886794
DOI: 10.1038/NATURE16952