Zinc in PDB 5f6k: Crystal Structure of the MLL3-ASH2L-RBBP5 Complex

All present enzymatic activity of Crystal Structure of the MLL3-ASH2L-RBBP5 Complex:
2.1.1.43;

The structure of Crystal Structure of the MLL3-ASH2L-RBBP5 Complex, PDB code: 5f6k 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)	44.42 / 2.41
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	80.342, 236.076, 44.416, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 22.8

The binding sites of Zinc atom in the Crystal Structure of the MLL3-ASH2L-RBBP5 Complex (pdb code 5f6k). 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 MLL3-ASH2L-RBBP5 Complex, PDB code: 5f6k:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the MLL3-ASH2L-RBBP5 Complex


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 MLL3-ASH2L-RBBP5 Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn5001 b:60.9 occ:1.00 SG C:CYS4901 2.3 57.0 1.0 SG C:CYS4851 2.4 62.8 1.0 SG C:CYS4899 2.4 67.6 1.0 SG C:CYS4906 2.4 57.5 1.0 CB C:CYS4901 3.4 65.4 1.0 CB C:CYS4906 3.5 61.0 1.0 CB C:CYS4851 3.5 64.4 1.0 CB C:CYS4899 3.6 69.7 1.0 N C:CYS4901 3.9 71.6 1.0 N C:CYS4851 3.9 55.6 1.0 N C:ARG4907 4.1 65.4 1.0 CA C:CYS4906 4.1 62.5 1.0 CA C:CYS4901 4.2 70.0 1.0 CA C:CYS4851 4.3 58.4 1.0 C C:CYS4906 4.6 62.2 1.0 N C:LYS4908 4.6 65.9 1.0 C C:CYS4899 4.6 75.7 1.0 CA C:CYS4899 4.8 73.0 1.0 N C:GLY4902 4.8 71.5 1.0 N C:HIS4900 4.8 73.2 1.0 C C:SER4850 4.9 53.6 1.0 C C:CYS4901 4.9 69.7 1.0 O C:CYS4899 4.9 80.6 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the MLL3-ASH2L-RBBP5 Complex


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 MLL3-ASH2L-RBBP5 Complex within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn5001 b:51.0 occ:1.00 SG E:CYS4901 2.3 48.8 1.0 SG E:CYS4906 2.3 55.9 1.0 SG E:CYS4899 2.3 48.5 1.0 SG E:CYS4851 2.4 47.3 1.0 CB E:CYS4906 3.3 47.4 1.0 CB E:CYS4901 3.4 47.6 1.0 CB E:CYS4899 3.5 54.1 1.0 CB E:CYS4851 3.6 49.6 1.0 CA E:CYS4906 3.9 52.3 1.0 N E:CYS4901 3.9 55.2 1.0 N E:CYS4851 3.9 45.1 1.0 N E:ARG4907 4.1 52.8 1.0 CA E:CYS4901 4.2 53.7 1.0 C E:CYS4899 4.4 59.6 1.0 CA E:CYS4851 4.4 44.7 1.0 O E:CYS4899 4.4 63.6 1.0 C E:CYS4906 4.4 53.7 1.0 CA E:CYS4899 4.6 56.6 1.0 N E:LYS4908 4.6 54.0 1.0 NE2 E:HIS4849 4.8 50.5 1.0 CD2 E:HIS4849 4.8 49.0 1.0 N E:HIS4900 4.8 56.9 1.0 C E:CYS4901 4.9 56.0 1.0 N E:GLY4902 4.9 53.2 1.0 C E:SER4850 5.0 43.4 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