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Atomistry » Zinc » PDB 1hxy-1i95 » 1i5o | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1hxy-1i95 » 1i5o » |
Zinc in PDB 1i5o: Crystal Structure of Mutant R105A of E. Coli Aspartate TranscarbamoylaseEnzymatic activity of Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase
All present enzymatic activity of Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase:
2.1.3.2; Protein crystallography data
The structure of Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase, PDB code: 1i5o
was solved by
C.P.Macol,
H.Tsuruta,
B.Stec,
E.R.Kantrowitz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase
(pdb code 1i5o). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase, PDB code: 1i5o: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1i5oGo back to Zinc Binding Sites List in 1i5o
Zinc binding site 1 out
of 2 in the Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 1i5oGo back to Zinc Binding Sites List in 1i5o
Zinc binding site 2 out
of 2 in the Crystal Structure of Mutant R105A of E. Coli Aspartate Transcarbamoylase
Mono view Stereo pair view
Reference:
C.P.Macol,
H.Tsuruta,
B.Stec,
E.R.Kantrowitz.
Direct Structural Evidence For A Concerted Allosteric Transition in Escherichia Coli Aspartate Transcarbamoylase. Nat.Struct.Biol. V. 8 423 2001.
Page generated: Wed Dec 16 02:52:19 2020
ISSN: ISSN 1072-8368 PubMed: 11323717 DOI: 10.1038/87582 |
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