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PDBsum entry 3bo5
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Contents |
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Crystal structure of methyltransferase domain of human histone-lysine n-methyltransferase setmar
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Structure:
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Histone-lysine n-methyltransferase setmar. Chain: a. Fragment: histone-lysine n-methyltransferase domain: residues 2-290. Synonym: set domain and mariner transposase fusion gene-containing protein, metnase, hsmar1 [includes: histone-lysine n- methyltransferase, and mariner transposase hsmar1]. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: setmar. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.59Å
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R-factor:
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0.157
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R-free:
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0.199
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Authors:
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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 Genomics Consortium (Sgc)
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Key ref:
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H.Wu
et al.
The crystal structure of methyltransferase domain of human histone-Lysine n-Methyltransferase setmar in complex with adohcy..
To be published,
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Date:
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17-Dec-07
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Release date:
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22-Jan-08
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PROCHECK
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Headers
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References
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Q53H47
(SETMR_HUMAN) -
Histone-lysine N-methyltransferase SETMAR from Homo sapiens
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Seq:
Struc:
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684 a.a.
269 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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Enzyme class 2:
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E.C.2.1.1.357
- [histone H3]-lysine(36) N-dimethyltransferase.
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Reaction:
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L-lysyl36-[histone H3] + 2 S-adenosyl-L-methionine = N6,N6- dimethyl-L-lysyl36-[histone H3] + 2 S-adenosyl-L-homocysteine + 2 H+
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L-lysyl(36)-[histone H3]
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+
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2
×
S-adenosyl-L-methionine
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=
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N(6),N(6)- dimethyl-L-lysyl(36)-[histone H3]
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+
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2
×
S-adenosyl-L-homocysteine
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+
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2
×
H(+)
Bound ligand (Het Group name = )
corresponds exactly
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Enzyme class 3:
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E.C.3.1.-.-
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Links
