Structure of PDB 7abr Chain E

Receptor sequence
>7abrE (length=571) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
ANTPTLDSLARDLTAIAKEDSLDPVIGRSKEIQRVIEVLSRRTKNNPVLI
GEPGVGKTAIAEGLAQQIINNEVPEILRDKRVMTLDMGTVVAGTKYRGEF
EDRLKKVMDEIRQAGNIILFIDALHTLIGAIDASNILKPSLARGELQCIG
ATTLDEYRKYIEKDAALERRFQPIQVDQPSVDESIQILQGLRDRYEAHHR
VSITDDAIEAAVKLSDRYISDRFLPDKAIDLIDEAGSKVRLRSFQENSEV
TVDDIAMVVSSWTGVPVSKIAQTETDKLLNMENILHSRVIGQDEAVVAVA
KAVRRARAGLKDPKRPIGSFIFLGPTGVGKTELARALAESIFGDEESMIR
IDMSEYMEKHSTSRLVGSPPGYVGYDEGGQLTEKVRRKPYSVVLLDAIEK
AHPDVFNILLQVLEDGRLTDSKGRTVDFRNTILIMTSNVGASEQNHKDMK
DKVMGELKRAFRPEFINRIDEIIVFHSLEKKHLTEIVSLMSDQLTKRLKE
QDLSIELTDAAKAKVAEEGVDLEYGARPLRRAIQKHVEDRLSEELLRGNI
HKGQHIVLDVEDGEFVVKTTA
3D structure
PDB7abr BacPROTACs mediate targeted protein degradation in bacteria.
ChainE
Resolution3.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 peptide E K252 Y253 R254 Y593 V594 K95 Y96 R97 Y372 V373
BS02 ATP E I511 T547 G548 V549 G550 K551 T552 E553 A762 R763 I290 T326 G327 V328 G329 K330 T331 E332 A526 R527
BS03 ATP E V182 I183 P210 G213 K214 T215 P388 I392 V25 I26 P53 G56 K57 T58 P225 I229
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0030420 establishment of competence for transformation

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Molecular Function
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Biological Process
External links
PDB RCSB:7abr, PDBe:7abr, PDBj:7abr
PDBsum7abr
PubMed35662409
UniProtP37571|CLPC_BACSU Negative regulator of genetic competence ClpC/MecB (Gene Name=clpC)

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