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Zinc in PDB 3s8p: Crystal Structure of the Set Domain of Human Histone-Lysine N- Methyltransferase SUV420H1 in Complex with S-Adenosyl-L-Methionine

Enzymatic activity of Crystal Structure of the Set Domain of Human Histone-Lysine N- Methyltransferase SUV420H1 in Complex with S-Adenosyl-L-Methionine

All present enzymatic activity of Crystal Structure of the Set Domain of Human Histone-Lysine N- Methyltransferase SUV420H1 in Complex with S-Adenosyl-L-Methionine:
2.1.1.43;

Protein crystallography data

The structure of Crystal Structure of the Set Domain of Human Histone-Lysine N- Methyltransferase SUV420H1 in Complex with S-Adenosyl-L-Methionine, PDB code: 3s8p was solved by R.Lam, H.Zeng, P.Loppnau, C.Bountra, J.Weigelt, C.H.Arrowsmith, A.M.Edwards, J.Min, H.Wu, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.94 / 1.85
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 46.424, 50.134, 74.839, 100.99, 108.05, 89.76
R / Rfree (%) 18.7 / 21.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Set Domain of Human Histone-Lysine N- Methyltransferase SUV420H1 in Complex with S-Adenosyl-L-Methionine (pdb code 3s8p). 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 Set Domain of Human Histone-Lysine N- Methyltransferase SUV420H1 in Complex with S-Adenosyl-L-Methionine, PDB code: 3s8p:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 3s8p

Go back to Zinc Binding Sites List in 3s8p
Zinc binding site 1 out of 2 in the Crystal Structure of the Set Domain of Human Histone-Lysine N- Methyltransferase SUV420H1 in Complex with S-Adenosyl-L-Methionine


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 Set Domain of Human Histone-Lysine N- Methyltransferase SUV420H1 in Complex with S-Adenosyl-L-Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:26.4
occ:1.00
SG A:CYS321 2.3 25.0 1.0
SG A:CYS319 2.3 23.3 1.0
SG A:CYS275 2.3 27.0 1.0
SG A:CYS324 2.4 25.8 1.0
CB A:CYS319 3.3 21.2 1.0
CB A:CYS324 3.3 26.4 1.0
CB A:CYS321 3.4 25.3 1.0
CB A:CYS275 3.5 27.0 1.0
N A:CYS275 3.9 25.1 1.0
N A:CYS324 4.0 25.4 1.0
N A:CYS321 4.0 25.0 1.0
NE2 A:HIS273 4.2 22.6 1.0
CA A:CYS324 4.2 26.9 1.0
CA A:CYS321 4.2 25.9 1.0
CA A:CYS275 4.3 25.3 1.0
CD2 A:HIS273 4.3 21.7 1.0
CA A:CYS319 4.5 23.7 1.0
O A:HOH346 4.6 35.4 1.0
C A:CYS319 4.6 25.1 1.0
O A:CYS321 4.8 27.8 1.0
C A:CYS321 4.8 28.5 1.0
O A:CYS319 4.8 25.7 1.0
C A:ASP274 4.8 24.9 1.0

Zinc binding site 2 out of 2 in 3s8p

Go back to Zinc Binding Sites List in 3s8p
Zinc binding site 2 out of 2 in the Crystal Structure of the Set Domain of Human Histone-Lysine N- Methyltransferase SUV420H1 in Complex with S-Adenosyl-L-Methionine


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 Set Domain of Human Histone-Lysine N- Methyltransferase SUV420H1 in Complex with S-Adenosyl-L-Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn400

b:28.7
occ:1.00
SG B:CYS275 2.2 29.0 1.0
SG B:CYS324 2.3 26.8 1.0
SG B:CYS321 2.3 26.4 1.0
SG B:CYS319 2.3 25.7 1.0
CB B:CYS324 3.2 27.8 1.0
CB B:CYS319 3.3 24.6 1.0
CB B:CYS275 3.4 29.0 1.0
CB B:CYS321 3.4 25.3 1.0
N B:CYS275 3.9 26.6 1.0
N B:CYS324 4.0 28.0 1.0
N B:CYS321 4.1 25.8 1.0
CE1 B:HIS273 4.1 21.7 1.0
CA B:CYS324 4.2 30.5 1.0
CA B:CYS275 4.2 28.0 1.0
CA B:CYS321 4.3 26.3 1.0
ND1 B:HIS273 4.3 22.5 1.0
O B:HOH347 4.4 33.6 1.0
CA B:CYS319 4.6 26.3 1.0
C B:CYS319 4.6 27.3 1.0
O B:CYS319 4.8 29.5 1.0
C B:CYS321 4.8 28.2 1.0
C B:ASP274 4.9 26.1 1.0
O B:CYS321 4.9 28.1 1.0

Reference:

H.Wu, A.Siarheyeva, H.Zeng, R.Lam, A.Dong, X.H.Wu, Y.Li, M.Schapira, M.Vedadi, J.Min. Crystal Structures of the Human Histone H4K20 Methyltransferases SUV420H1 and SUV420H2. Febs Lett. V. 587 3859 2013.
ISSN: ISSN 0014-5793
PubMed: 24396869
Page generated: Sat Oct 26 15:36:24 2024

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