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PDBsum entry 1moo
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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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The refined atomic structure of carbonic anhydrase ii at 1.05 a resolution: implications of chemical rescue of proton transfer.
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Authors
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D.Duda,
L.Govindasamy,
M.Agbandje-Mckenna,
C.Tu,
D.N.Silverman,
R.Mckenna.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2003,
59,
93.
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PubMed id
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Abstract
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Using synchrotron radiation and a CCD detector, X-ray data have been collected
at 100 K for the His64Ala mutant of human carbonic anhydrase II complexed with
4-methylimidazole (4-MI) to a maximal 1.05 A resolution, allowing full
anisotropic least-squares refinement. The refined model has a conventional R
factor of 15.7% for all reflections. The C(alpha) coordinates of the model
presented here have an r.m.s. deviation of 0.10 A relative to the previously
determined structure at 1.6 A resolution. Several amino-acid residues (six of
the 255 observed) have been identified with multiple rotamer side-chain
conformations. C, N and O atoms can be differentiated with selective
electron-density map contouring. The estimated standard deviations for all
main-chain non-H atom bond lengths and angles are 0.013 and 0.030 A,
respectively, based on unrestrained full-matrix least-squares refinement. This
structure gives detailed information about the tetrahedrally arranged zinc ion
coordinated by three histidine N atoms (His94 N(epsilon 2), His96 N(epsilon2)
and His119 N(delta1)) and a water/hydroxide, the multiple binding sites of the
proton chemical rescue molecule 4-MI and the solvent networks linking the
zinc-bound water/hydroxide and 4-MI molecules. This structure presents the
highest resolution structure of a carbonic anhydrase isozyme so far determined
and adds to the understanding of proton-transfer processes.
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Secondary reference #1
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Title
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Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrase ii.
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Authors
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D.Duda,
C.Tu,
M.Qian,
P.Laipis,
M.Agbandje-Mckenna,
D.N.Silverman,
R.Mckenna.
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Ref.
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Biochemistry, 2001,
40,
1741-1748.
[DOI no: ]
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PubMed id
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