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PDBsum entry 3dnm
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References listed in PDB file
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Key reference
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Title
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Structural and functional analysis of a novel hormone-Sensitive lipase from a metagenome library.
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Authors
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K.H.Nam,
M.Y.Kim,
S.J.Kim,
A.Priyadarshi,
S.T.Kwon,
B.S.Koo,
S.H.Yoon,
K.Y.Hwang.
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Ref.
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Proteins, 2009,
74,
1036-1040.
[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. Biological and structural analysis of EstE7. (a)
Relative activity of recombinant EstE7 toward p-nitrophenyl
esters. Esterase activity was determined photometrically in a 50
mM Tris-HCl buffer (pH 7.5) using various p-nitrophenyl esters
as substrates. (b) The EstE7 monomer structure has two domains:
an  /
 domain
(green) and a regulatory domain (blue). The catalytic triad
residues are shown in ball-and-stick representations. (c)
Nucleophile Ser157 in molecule A interact with -mercaptoethanol.
The catalytic site consists of three residues: Ser157
(nucleophile), Glu251 (charge-relay network), and His281 (proton
carrier). -mercaptoethanol
is shown in ball-and-stick representations.  A
weighted electron density maps (2Fo - Fc) contoured at 1 in
the vicinity of catalytic residues and -mercaptoethanol.
(d) Substrate-binding tunnel. This tunnel of the hydrophobic
pocket has an ovoidal shape with approximate depth of  16
Å. The nucleophile Ser157 residue is shown in
ball-and-stick representations in the area of the orange dotted
circle.
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The above figure is
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2009,
74,
1036-1040)
copyright 2009.
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