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protein links
Transferase PDB id
3dlm
Jmol
Contents
Protein chain
208 a.a. *
Waters ×212
* Residue conservation analysis
PDB id:
3dlm
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
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q15047  (SETB1_HUMAN) -  Histone-lysine N-methyltransferase SETDB1
Seq:
Struc:
 
Seq:
Struc:
 
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 reactions 
   Enzyme class: E.C.2.1.1.43  - Histone-lysine N-methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      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 
  GO annot!
  Biochemical function     nucleic acid binding     1 term