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PDBsum entry 3grf
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References listed in PDB file
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Key reference
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Title
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X-Ray structure and kinetic properties of ornithine transcarbamoylase from the human parasite giardia lamblia.
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Authors
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A.Galkin,
L.Kulakova,
R.Wu,
M.Gong,
D.Dunaway-Mariano,
O.Herzberg.
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Ref.
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Proteins, 2009,
76,
1049-1053.
[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. Overall fold, active site architecture of glOTC, and
sequence alignment of glOTC and hOTC. (A) Ribbon diagram
representation of the protein trimer. The Ni^2+ ion at the
center of the trimer is shown as magenta sphere. (B)
Stereoscopic view of the glOTC active site superposed with the
hOTC/PALO active site. The carbon atoms are colored green
(glOTC) and magenta (hOTC). Other atomic colors are as follows:
oxygen, red; nitrogen, blue; phosphor, orange; and sulfur,
yellow. Black residue labels correspond to glOTC, except that
the two residues labeled in magenta color (His117 of a
neighboring subunit and Met268) are hOTC residues that are
disordered in the glOTC structure (Ser82 and Tyr245,
respectively). (C) Sequence alignment of glOTC and hOTC.
Identical residues are blocked in blue and residues surrounding
the active site are indicated by red triangles.
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The above figure is
reprinted
from an Open Access publication published by John Wiley & Sons, Inc.:
Proteins
(2009,
76,
1049-1053)
copyright 2009.
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