DNA Binding Motif

						

			
Accessions: 1lli_AB (3D-footprint 20231221)

			
Names: PROTEIN (LAMBDA REPRESSOR)
Organisms: Enterobacteria phage lambda, Escherichia phage lambda
Libraries: 3D-footprint 20231221 1
1 Contreras-Moreira B. 3D-footprint: a database for the structural analysis of protein-DNA complexes. Nucleic acids research 38:D91-7 (2010). [Pubmed]
Description: THE CRYSTAL STRUCTURE OF A MUTANT PROTEIN WITH ALTERED BUT IMPROVED HYDROPHOBIC CORE PACKING
Length: 17
Consensus: TAnCAmTnGsGGtGaTA
Weblogo: 
PSSM: P0      A      C      G      T
01      0      0      0     96      T
02     96      0      0      0      A
03     24     24     24     24      n
04      0     96      0      0      C
05     67     16      9      4      A
06     32     64      0      0      m
07      0      0      0     96      T
08     24     24     24     24      n
09      0      0     96      0      G
10      4     50     33      9      s
11      0      0     96      0      G
12      0      0     96      0      G
13      4     16     12     64      t
14      0      0     96      0      G
15     64      9     16      7      a
16      0      0      0     96      T
17     81      4      4      7      A
Type: Heterodimer
Binding TFs: 1lli_A (Helix-turn-helix)
1lli_B (Helix-turn-helix)
Binding Sites: 1lli_D
1lli_E
			
Publications: Lim W.A, Hodel A, Sauer R.T, Richards F.M. The crystal structure of a mutant protein with altered but improved hydrophobic core packing. Proceedings of the National Academy of Sciences of the United States of America 91:423-7 (1994). [Pubmed]

	
			


			

				

				
				
				
				

			

			

		

	
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These data are available AS IS and at your own risk. The EEAD/CSIC do not give any representation or warranty nor assume any liability or responsibility for the data nor the results posted (whether as to their accuracy, completeness, quality or otherwise). Access to these data is available free of charge for ordinary use in the course of research. Downloaded data have CC-BY-NC-SA license. FootprintDB is also available at RSAT::Plants, part of the INB/ELIXIR-ES resources portfolio.