 |
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
PDB id:
|
 |
|
 |
| Name: |
 |
Transferase
|
 |
|
Title:
|
 |
Crystal structure of tudor domain of human histone-lysine n- methyltransferase setdb1
|
|
Structure:
|
 |
Histone-lysine n-methyltransferase setdb1. Chain: a. Synonym: set domain bifurcated 1, erg-associated protein with set domain, eset, histone h3-k9 methyltransferase 4, h3-k9-hmtase 4, lysine n- methyltransferase 1e. Engineered: yes. Mutation: yes
|
|
Source:
|
 |
Homo sapiens. Organism_taxid: 9606. Gene: setdb1, kiaa0067, kmt1e. Expressed in: escherichia coli.
|
|
Resolution:
|
 |
|
1.77Å
|
R-factor:
|
0.210
|
R-free:
|
0.237
|
|
|
Authors:
|
 |
M.F.Amaya,L.Dombrovski,P.Loppnau,C.Bountra,J.Weigelt, C.H.Arrowsmith,A.M.Edwards,A.Bochkarev,J.Min,H.Wu, Structural Genomics Consortium (Sgc)
|
|
Key ref:
|
 |
L.Dombrovski
et al.
The crystal structure of tudor domain of human histone-Lysine n-Methyltransferase setdb1..
To be published,
|
 |
|
Date:
|
 |
|
27-Jun-08
|
Release date:
|
12-Aug-08
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
Headers
|
 |
|
|
References
|
|
|
|
|
|
|
|
|
|
Q15047
(SETB1_HUMAN) -
Histone-lysine N-methyltransferase SETDB1
|
|
|
|
Seq: Struc:
|
 |
 |
 |
1291 a.a.
208 a.a.*
|
|
|
|
|
|
|
 |
 |
|
|
Key: |
 |
PfamA domain |
 |
 |
PfamB domain |
 |
 |
 |
Secondary structure |
 |
|
*
PDB and UniProt seqs differ
at 5 residue positions (black
crosses)
|
|
|
|
|
 |
|
|
 |
 |
 |
 |
Enzyme class:
|
 |
E.C.2.1.1.43
- Histone-lysine N-methyltransferase.
|
|
 |
 |
 |
 |
 |
Reaction:
|
 |
S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N6-methyl-L-lysine-[histone]
|
 |
 |
 |
 |
 |
S-adenosyl-L-methionine
|
+
|
L-lysine-[histone]
|
=
|
S-adenosyl-L-homocysteine
|
+
|
N(6)-methyl-L-lysine-[histone]
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
|
|
 |
 |
|
 |
|
 |
|
|
Gene Ontology (GO) functional annotation
|
|
|
|
 |
 |
 |
|
 |
 |
 |
 |
|
 |
|
Biochemical function
|
nucleic acid binding
|
1 term
|
 |
|
|
 |
 |
 |
 |
 |
 |
|