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PDBsum entry 1moo
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Contents |
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* Residue conservation analysis
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Enzyme class 2:
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E.C.4.2.1.1
- carbonic anhydrase.
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Reaction:
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hydrogencarbonate + H+ = CO2 + H2O
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hydrogencarbonate
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+
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H(+)
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=
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CO2
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+
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H2O
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Cofactor:
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Zn(2+)
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Enzyme class 3:
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E.C.4.2.1.69
- cyanamide hydratase.
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Reaction:
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urea = cyanamide + H2O
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urea
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=
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cyanamide
Bound ligand (Het Group name = )
matches with 50.00% similarity
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+
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H2O
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Acta Crystallogr D Biol Crystallogr
59:93
(2003)
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PubMed id:
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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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D.Duda,
L.Govindasamy,
M.Agbandje-McKenna,
C.Tu,
D.N.Silverman,
R.McKenna.
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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.M.Maupin,
R.McKenna,
D.N.Silverman,
and
G.A.Voth
(2009).
Elucidation of the proton transport mechanism in human carbonic anhydrase II.
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J Am Chem Soc,
131,
7598-7608.
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S.Z.Fisher,
A.Y.Kovalevsky,
J.F.Domsic,
M.Mustyakimov,
D.N.Silverman,
R.McKenna,
and
P.Langan
(2009).
Preliminary joint neutron and X-ray crystallographic study of human carbonic anhydrase II.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
65,
495-498.
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C.M.Maupin,
M.G.Saunders,
I.F.Thorpe,
R.McKenna,
D.N.Silverman,
and
G.A.Voth
(2008).
Origins of enhanced proton transport in the Y7F mutant of human carbonic anhydrase II.
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J Am Chem Soc,
130,
11399-11408.
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F.Bootorabi,
J.Jänis,
J.Valjakka,
S.Isoniemi,
P.Vainiotalo,
D.Vullo,
C.T.Supuran,
A.Waheed,
W.S.Sly,
O.Niemelä,
and
S.Parkkila
(2008).
Modification of carbonic anhydrase II with acetaldehyde, the first metabolite of ethanol, leads to decreased enzyme activity.
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BMC Biochem,
9,
32.
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V.M.Krishnamurthy,
G.K.Kaufman,
A.R.Urbach,
I.Gitlin,
K.L.Gudiksen,
D.B.Weibel,
and
G.M.Whitesides
(2008).
Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
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Chem Rev,
108,
946.
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C.M.Maupin,
and
G.A.Voth
(2007).
Preferred orientations of His64 in human carbonic anhydrase II.
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Biochemistry,
46,
2938-2947.
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D.Bhatt,
S.Z.Fisher,
C.Tu,
R.McKenna,
and
D.N.Silverman
(2007).
Location of binding sites in small molecule rescue of human carbonic anhydrase II.
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Biophys J,
92,
562-570.
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PDB codes:
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J.M.Swanson,
C.M.Maupin,
H.Chen,
M.K.Petersen,
J.Xu,
Y.Wu,
and
G.A.Voth
(2007).
Proton solvation and transport in aqueous and biomolecular systems: insights from computer simulations.
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J Phys Chem B,
111,
4300-4314.
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M.Budayova-Spano,
S.Z.Fisher,
M.T.Dauvergne,
M.Agbandje-McKenna,
D.N.Silverman,
D.A.Myles,
and
R.McKenna
(2006).
Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
62,
6-9.
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PDB code:
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P.Venkataraman,
R.A.Lamb,
and
L.H.Pinto
(2005).
Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virus.
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J Biol Chem,
280,
21463-21472.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
