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

Enzymatic activity of 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;

Protein crystallography data

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

Zinc Binding Sites:

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 5f6k

Go back to Zinc Binding Sites List in 5f6k
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 5f6k

Go back to Zinc Binding Sites List in 5f6k
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

Reference:

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
Page generated: Sun Oct 27 15:49:16 2024

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