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PDBsum entry 2fa5

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Top Page protein metals Protein-protein interface(s) links
Transcription PDB id
2fa5
Contents
Protein chains
139 a.a.
Metals
_CL ×2
Waters ×313

References listed in PDB file
Key reference
Title The crystal structure of xc1739: a putative multiple antibiotic-Resistance repressor (marr) from xanthomonas campestris at 1.8 a resolution.
Authors K.H.Chin, Z.L.Tu, J.N.Li, C.C.Chou, A.H.Wang, S.H.Chou.
Ref. Proteins, 2006, 65, 239-242. [DOI no: 10.1002/prot.21017]
PubMed id 16862595
Abstract
No abstract given.
Figure 1.
Figure 1. (a) Sequence alignment of XC1739 with E. coli. MarR. The secondary structure elements were illustrated as green tubes for -helices and red arrows for -strands; the wing region was drawn as gray lines. Numbering starts according to the XC1739 primary sequence. Residues that are identical between the two sequences are colored in red, highly conserved in blue. Residues that are conserved and important in stabilizing dimerization domains are marked with a plus sign, while those important in forming hydrophobic core for each individual DNA-binding domain are denoted with an asterisk sign. (b) Ribbon representation of the XC1739 structural dimer. The secondary structures are colored coded from N-terminal to C-terminal in blue and green, and green and red, respectively, for each momoner. The electron density of the wing region is invisible and was marked as gray dots. (c) Stereodiagram of the electrostatic surface map of the XC1739 dimer. Positive charged residues are coded in blue and negative residues in red. (d) Superimposition diagram of the XC1739 dimer (colored in blue) with the liganded E. coli MarR dimer (colored in red). The diagrams are prepared using PdbViewer[18] except panel c, which is drawn using PyMol (DeLano Scientific LLC).
The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2006, 65, 239-242) copyright 2006.
PROCHECK
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