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PDBsum entry 1vj1
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Unknown function
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PDB id
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1vj1
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of a putative NADPH-Dependent oxidoreductase (gi: 18204011) from mouse at 2.10 a resolution.
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Authors
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I.Levin,
R.Schwarzenbacher,
D.Mcmullan,
P.Abdubek,
E.Ambing,
T.Biorac,
J.Cambell,
J.M.Canaves,
H.J.Chiu,
X.Dai,
A.M.Deacon,
M.Didonato,
M.A.Elsliger,
A.Godzik,
C.Grittini,
S.K.Grzechnik,
E.Hampton,
L.Jaroszewski,
C.Karlak,
H.E.Klock,
E.Koesema,
A.Kreusch,
P.Kuhn,
S.A.Lesley,
T.M.Mcphillips,
M.D.Miller,
A.Morse,
K.Moy,
J.Ouyang,
R.Page,
K.Quijano,
R.Reyes,
A.Robb,
E.Sims,
G.Spraggon,
R.C.Stevens,
H.Van den bedem,
J.Velasquez,
J.Vincent,
F.Von delft,
X.Wang,
B.West,
G.Wolf,
Q.Xu,
K.O.Hodgson,
J.Wooley,
I.A.Wilson.
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Ref.
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Proteins, 2004,
56,
629-633.
[DOI no: ]
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PubMed id
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Abstract
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No abstract given.
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Figure 1.
Figure 1. Crystal structure of 18204011. A: Stereo ribbon
diagram of mouse 18204011 color-coded from N-terminus (blue) to
C-terminus (red) showing the domain organization and location of
the putative active site (arrow). Helices H1-H17, and  -strands
( 1-
15)
as well as -sheets
A, B, C and beginning (C253) and end (P266) of the disordered
loop are indicated. B: Diagram showing the secondary structure
elements in 18204011 superimposed on its primary sequence. The
strands in each -sheet
are indicated by a red A, B, and C. -hairpins
are depicted as red loops. Disordered regions are depicted by a
dashed line with the corresponding sequence in brackets. -bulges
are marked by ;
 -turns
are marked by .
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Figure 2.
Figure 2. A: Ribbon diagram of a superposition of 18204011
(mouse) and quinone oxidoreductase from E. coli (PDB: 1qor)
grey. The structures were superimposed on their
nucleotide-binding domains. The NADPH molecule bound to quinone
oxidoreductase is shown in cpk mode. B: Close up view of the
active site. The NADPH molecule and the sulfate bound to the
active site of quinone oxidoreductase are shown in ball and
stick. The active site tyrosine (Y52) as observed in quinone
oxidoreductase from E. coli and its potential counterpart (Y64)
in 18204011 (the Y64 side-chain has been modeled here due to
disorder in the crystal structure) are shown in ball and stick.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2004,
56,
629-633)
copyright 2004.
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