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Zinc in PDB 2w5z: Ternary Complex of the Mixed Lineage Leukaemia (MLL1) Set Domain with the Cofactor Product S-Adenosylhomocysteine and Histone Peptide.

Enzymatic activity of Ternary Complex of the Mixed Lineage Leukaemia (MLL1) Set Domain with the Cofactor Product S-Adenosylhomocysteine and Histone Peptide.

All present enzymatic activity of Ternary Complex of the Mixed Lineage Leukaemia (MLL1) Set Domain with the Cofactor Product S-Adenosylhomocysteine and Histone Peptide.:
2.1.1.43;

Protein crystallography data

The structure of Ternary Complex of the Mixed Lineage Leukaemia (MLL1) Set Domain with the Cofactor Product S-Adenosylhomocysteine and Histone Peptide., PDB code: 2w5z was solved by S.M.Southall, P.S.Wong, Z.Odho, S.M.Roe, J.R.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.52 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.950, 56.550, 78.410, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 24.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Ternary Complex of the Mixed Lineage Leukaemia (MLL1) Set Domain with the Cofactor Product S-Adenosylhomocysteine and Histone Peptide. (pdb code 2w5z). 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 Ternary Complex of the Mixed Lineage Leukaemia (MLL1) Set Domain with the Cofactor Product S-Adenosylhomocysteine and Histone Peptide., PDB code: 2w5z:

Zinc binding site 1 out of 1 in 2w5z

Go back to Zinc Binding Sites List in 2w5z
Zinc binding site 1 out of 1 in the Ternary Complex of the Mixed Lineage Leukaemia (MLL1) Set Domain with the Cofactor Product S-Adenosylhomocysteine and Histone Peptide.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Ternary Complex of the Mixed Lineage Leukaemia (MLL1) Set Domain with the Cofactor Product S-Adenosylhomocysteine and Histone Peptide. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn4970

b:44.4
occ:1.00
 SG A:CYS3959 2.3 36.7 1.0
SG A:CYS3957 2.3 36.2 1.0
SG A:CYS3909 2.5 46.0 1.0
SG A:CYS3964 2.6 48.3 1.0
CB A:CYS3959 3.4 25.7 1.0
CB A:CYS3909 3.5 35.5 1.0
CB A:CYS3957 3.5 41.2 1.0
CB A:CYS3964 3.5 52.0 1.0
CA A:CYS3964 3.8 59.6 1.0
N A:CYS3909 3.9 37.6 1.0
N A:CYS3959 4.0 34.1 1.0
N A:ARG3965 4.0 48.0 1.0
CA A:CYS3959 4.2 33.3 1.0
O A:HOH2055 4.3 53.4 1.0
CA A:CYS3909 4.3 38.6 1.0
C A:CYS3964 4.4 43.2 1.0
NE2 A:HIS3907 4.5 41.6 1.0
CD2 A:HIS3907 4.6 25.1 1.0
C A:CYS3957 4.6 39.0 1.0
N A:LYS3966 4.7 52.9 1.0
CA A:CYS3957 4.7 37.9 1.0
O A:CYS3957 4.7 40.0 1.0
N A:GLY3960 4.8 48.1 1.0
C A:CYS3959 4.9 42.5 1.0
C A:SER3908 4.9 50.7 1.0

Reference:

S.M.Southall, P.S.Wong, Z.Odho, S.M.Roe, J.R.Wilson. Structural Basis For the Requirement of Additional Factors For MLL1 Set Domain Activity and Recognition of Epigenetic Marks. Mol.Cell V. 33 181 2009.
ISSN: ISSN 1097-2765
PubMed: 19187761
DOI: 10.1016/J.MOLCEL.2008.12.029
Page generated: Thu Oct 17 04:46:21 2024

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