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PDBsum entry 3mqm
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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 the bromodomain of human ash1l
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Structure:
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Probable histone-lysine n-methyltransferase ash1l. Chain: a, b. Fragment: bromodomain of human ash1l (unp residues 2438:2564). Synonym: absent small and homeotic disks protein 1 homolog, ash1-like protein, huash1, lysine n-methyltransferase 2h. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ash1l, kiaa1420, kmt2h. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.54Å
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R-factor:
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0.207
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R-free:
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0.259
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Authors:
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P.Filippakopoulos,S.Picaud,T.Keates,I.Felletar,M.Vollmar,A.Chaikuad, T.Krojer,P.Canning,F.Von Delft,C.H.Arrowsmith,A.M.Edwards,J.Weigelt, C.Bountra,S.Knapp,Structural Genomics Consortium (Sgc)
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Key ref:
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P.Filippakopoulos
et al.
(2012).
Histone recognition and large-scale structural analysis of the human bromodomain family.
Cell,
149,
214-231.
PubMed id:
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Date:
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28-Apr-10
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Release date:
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19-May-10
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PROCHECK
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Headers
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References
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Q9NR48
(ASH1L_HUMAN) -
Histone-lysine N-methyltransferase ASH1L from Homo sapiens
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Seq:
Struc:
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2969 a.a.
126 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 1:
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E.C.2.1.1.359
- [histone H3]-lysine(36) N-trimethyltransferase.
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Reaction:
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L-lysyl36-[histone H3] + 3 S-adenosyl-L-methionine = N6,N6,N6- trimethyl-L-lysyl36-[histone H3] + 3 S-adenosyl-L-homocysteine + 3 H+
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L-lysyl(36)-[histone H3]
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+
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3
×
S-adenosyl-L-methionine
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=
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N(6),N(6),N(6)- trimethyl-L-lysyl(36)-[histone H3]
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+
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3
×
S-adenosyl-L-homocysteine
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+
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3
×
H(+)
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Enzyme class 2:
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E.C.2.1.1.367
- [histone H3]-lysine(9) N-methyltransferase.
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Reaction:
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L-lysyl9-[histone H3] + S-adenosyl-L-methionine = N6-methyl-L- lysyl9-[histone H3] + S-adenosyl-L-homocysteine + H+
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L-lysyl(9)-[histone H3]
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+
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3
×
S-adenosyl-L-methionine
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=
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N(6)-methyl-L- lysyl(9)-[histone H3]
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+
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3
×
S-adenosyl-L-homocysteine
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+
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3
×
H(+)
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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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Cell
149:214-231
(2012)
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PubMed id:
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Histone recognition and large-scale structural analysis of the human bromodomain family.
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P.Filippakopoulos,
S.Picaud,
M.Mangos,
T.Keates,
J.P.Lambert,
D.Barsyte-Lovejoy,
I.Felletar,
R.Volkmer,
S.Müller,
T.Pawson,
A.C.Gingras,
C.H.Arrowsmith,
S.Knapp.
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ABSTRACT
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.A.Musselman,
M.E.Lalonde,
J.Côté,
and
T.G.Kutateladze
(2012).
Perceiving the epigenetic landscape through histone readers.
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Nat Struct Mol Biol,
19,
1218-1227.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
