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PDBsum entry 4e2f
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Transferase/protein binding
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PDB id
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4e2f
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Contents |
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(+ 0 more)
310 a.a.
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(+ 0 more)
144 a.a.
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PDB id:
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Transferase/protein binding
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Title:
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Crystal structure of e. Coli aspartate transcarbamoylase k164e/e239k mutant in an intermediate state
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Structure:
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Aspartate carbamoyltransferase catalytic chain. Chain: i, k, g, c, a, e. Synonym: aspartate transcarbamylase, atcase. Engineered: yes. Mutation: yes. Aspartate carbamoyltransferase regulatory chain. Chain: d, b, j, l, h, f. Engineered: yes
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Source:
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Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: b4245, jw4204, pyrb. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: b4244, jw4203, pyri.
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Resolution:
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2.80Å
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R-factor:
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0.217
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R-free:
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0.274
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Authors:
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W.Guo,E.R.Kantrowitz
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Key ref:
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W.Guo
et al.
(2012).
Trapping and structure determination of an intermediate in the allosteric transition of aspartate transcarbamoylase.
Proc Natl Acad Sci U S A,
109,
7741-7746.
PubMed id:
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Date:
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08-Mar-12
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Release date:
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02-May-12
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PROCHECK
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Headers
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References
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Enzyme class 2:
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Chains I, K, G, C, A, E:
E.C.2.1.3.2
- aspartate carbamoyltransferase.
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Pathway:
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Pyrimidine Biosynthesis
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Reaction:
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carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H+
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carbamoyl phosphate
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+
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L-aspartate
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=
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N-carbamoyl-L-aspartate
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+
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phosphate
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+
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H(+)
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Enzyme class 3:
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Chains D, B, J, L, H, F:
E.C.?
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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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Proc Natl Acad Sci U S A
109:7741-7746
(2012)
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PubMed id:
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Trapping and structure determination of an intermediate in the allosteric transition of aspartate transcarbamoylase.
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W.Guo,
J.M.West,
A.S.Dutton,
H.Tsuruta,
E.R.Kantrowitz.
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ABSTRACT
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');
}
}
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