Structure of PDB 3jsp Chain B

Receptor sequence
>3jspB (length=192) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
KALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALA
RKGVIEIVSGASRGIRLLQEGLPLVGRVLAQQHIEGHYQVDPSLFKPNAD
FLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVARLKK
QGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL
3D structure
PDB3jsp Structure of the LexA-DNA complex and implications for SOS box measurement.
ChainB
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M118 S119 E152 A156
Catalytic site (residue number reindexed from 1) M108 S109 E142 A146
Enzyme Commision number 3.4.21.88: repressor LexA.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 dna B T27 R28 N41 E44 K48 S63 R64 T26 R27 N40 E43 K47 S62 R63 PDBbind-CN: Kd=1.59nM
BS02 dna B T5 R7 Q8 F37 R38 S39 N41 A42 E45 H46 R52 S63 T4 R6 Q7 F36 R37 S38 N40 A41 E44 H45 R51 S62 PDBbind-CN: Kd=1.59nM
Gene Ontology
Molecular Function
GO:0000976 transcription cis-regulatory region binding
GO:0001217 DNA-binding transcription repressor activity
GO:0003677 DNA binding
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0016787 hydrolase activity
GO:0042802 identical protein binding
Biological Process
GO:0006260 DNA replication
GO:0006281 DNA repair
GO:0006351 DNA-templated transcription
GO:0006355 regulation of DNA-templated transcription
GO:0006508 proteolysis
GO:0006974 DNA damage response
GO:0009432 SOS response
GO:0045892 negative regulation of DNA-templated transcription
Cellular Component
GO:0005829 cytosol
GO:0032993 protein-DNA complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3jsp, PDBe:3jsp, PDBj:3jsp
PDBsum3jsp
PubMed20703307
UniProtP0A7C2|LEXA_ECOLI LexA repressor (Gene Name=lexA)

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