PDBsum entry: 3bo5

Transferase

PDB id: 3bo5

Contents

Protein chain

269 a.a. *

Ligands

SAH

GOL ×2

Metals

_ZN ×4

Waters ×304

* Residue conservation analysis

PDB id:

3bo5

Name:

Transferase

Title:

Crystal structure of methyltransferase domain of human histo n-methyltransferase setmar

Structure:

Histone-lysine n-methyltransferase setmar. Chain: a. Fragment: histone-lysine n-methyltransferase domain: residu synonym: set domain and mariner transposase fusion gene-con protein, metnase, hsmar1 [includes: histone-lysine n- methyltransferase, and mariner transposase hsmar1]. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: setmar. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.59Å R-factor: 0.157 R-free: 0.199

Authors:

V.V.Lunin,H.Wu,H.Ren,E.Dobrovetsky,J.Weigelt,C.H.Arrowsmith, A.M.Edwards,A.Bochkarev,J.Min,A.N.Plotnikov,Structural Geno Consortium (Sgc)

Key ref:

H.Wu et al. The crystal structure of methyltransferase domain of human histone-Lysine n-Methyltransferase setmar in complex with adohcy.. To be published,

Date:

17-Dec-07 Release date: 22-Jan-08

Protein chain

Q53H47  (SETMR_HUMAN) -  Histone-lysine N-methyltransferase SETMAR

Seq: 671 a.a.

Struc: 269 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• 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 (Bound ligand (Het Group name = SAH) corresponds exactly) + N(6)-methyl-L-lysine-[histone]

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: nucleus (1 term)
• Biological process: histone lysine methylation (1 term)
• Biochemical function: protein binding (3 terms)