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PDBsum entry 3ng2
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Metal binding protein
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PDB id
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3ng2
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.2.3.2.27
- RING-type E3 ubiquitin transferase.
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Reaction:
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S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6- ubiquitinyl-[acceptor protein]-L-lysine
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Biochem J
431:23-29
(2010)
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PubMed id:
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RING domain dimerization is essential for RNF4 function.
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C.W.Liew,
H.Sun,
T.Hunter,
C.L.Day.
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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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A.Plechanovová,
E.G.Jaffray,
M.H.Tatham,
J.H.Naismith,
and
R.T.Hay
(2012).
Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis.
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Nature,
489,
115-120.
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PDB code:
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A.Plechanovová,
E.G.Jaffray,
S.A.McMahon,
K.A.Johnson,
I.Navrátilová,
J.H.Naismith,
and
R.T.Hay
(2011).
Mechanism of ubiquitylation by dimeric RING ligase RNF4.
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Nat Struct Mol Biol,
18,
1052-1059.
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PDB code:
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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.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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