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PDBsum entry 3ch4
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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 human phosphomevalonate kinase at 1.8 a resolution.
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Authors
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Q.Chang,
X.X.Yan,
S.Y.Gu,
J.F.Liu,
D.C.Liang.
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Ref.
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Proteins, 2008,
73,
254-258.
[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. A: Stereo ribbon representation of hPMK. The
different regions of the enzyme are color-coded. CORE region is
shown in magenta, LID region in green, and substrate binding
region in light brown. MPD (cyan) and sulfate ions (orange) are
shown in stick models. The P-loop is shown in dark blue. B:
Stereo ribbon representation of the superposition of DNK
(deoxynucleoside monophosphate kinase from Bacteriophage T4,
PDB: 1dek) with hPMK. DNK is shown in yellow and PMK in purple.
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Figure 2.
Figure 2. A: A superimposed view of the ATP binding site of
sulfate-bound PMK (purple), ATP-bound GntK (orange), and
ATP-bound DCK (green). The superimposition is based on C atoms
of the P-loop, helix 1
and strand 1.
ATP, MPD and sulfate ion are shown in stick models. B: The
interactions with the bounded sulfate ion and the interactions
between residues located in the P-loop and LID region. The
sulfate ion (SO[4]) and correlative residues are represented by
stick structures, and the remainder of the structure is shown in
cartoon representation. Carbon atoms are colored in purple,
oxygen atoms in red, nitrogen atoms in blue and the sulfur atom
is yellow. Hydrogen bond pairs are connected with green dashed
lines. C: Electrostatic surface representation of hPMK with the
transparent ribbon presentation. Red represents a negative
charge, and blue represents a positive charge. MPD and sulfate
ion are represented by sticks. The ATP-binding site is the
region within the cyan ellipse, and the substrate-binding site
is the region within the white rectangle. An enlarged view of
the detailed putative substrate-binding site is shown on the
right, and the conserved residues that may interact with
mevalonate 5-phosphate are shown by stick structures.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2008,
73,
254-258)
copyright 2008.
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