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PDBsum entry 3dwy
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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 crebbp
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Structure:
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Creb-binding protein. Chain: a, b. Fragment: bromo domain: residues 1084-1197. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: crebbp, cbp. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.98Å
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R-factor:
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0.162
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R-free:
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0.219
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Authors:
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P.Filippakopoulos,S.Picaud,O.Fedorov,R.Karim,A.C.W.Pike,F.Von Delft, C.H.Arrowsmith,A.M.Edwards,M.Wickstroem,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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23-Jul-08
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Release date:
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05-Aug-08
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PROCHECK
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Headers
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References
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Q92793
(CBP_HUMAN) -
CREB-binding protein from Homo sapiens
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Seq:
Struc:
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2442 a.a.
114 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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Enzyme class 1:
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E.C.2.3.1.-
- ?????
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Enzyme class 2:
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E.C.2.3.1.48
- histone acetyltransferase.
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Reaction:
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L-lysyl-[protein] + acetyl-CoA = N6-acetyl-L-lysyl-[protein] + CoA + H+
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L-lysyl-[protein]
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+
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acetyl-CoA
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=
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N(6)-acetyl-L-lysyl-[protein]
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+
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CoA
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+
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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
