BioLiP

Receptor Information

>6wqh Chain B (length=537) Species: 172827 (Meiothermus taiwanensis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

SDLEALRKKIEEVGMPEAVKTKALKELDRLERMQQGSPEATVARTYLDWL
TEVPWSKADPEVLDINHTRQVLDEDHYGLKDVKERILEYLAVRQLTQGLD
VRNKAPILVLVGPPGVGKTSLGRSIARSMNRKFHRISLGGVRDEAEIRGH
RRTYIGAMPGKLIHAMKQVGVINPVILLDEIDKMSSDWRGDPASAMLEVL
DPEQNNTFTDHYLDVPYDLSKVFFITTANTLQTIPRPLLDRMEVIEIPGY
TNMEKQAIARQYLWPKQVRESGMEGRIEVTDAAILRVISEYTREAGVRGL
ERELGKIARKGAKFWLEGAWEGLRTIDASDIPTYLGIPRYRPDKAETEPQ
VGTAQGLAWTPVGGTLLTIEVAAVPGSGKLSLTGQLGEVMKESAQAALTY
LRAHTQDYGLPEDFYNKVDLHVHVPDGATPKDGPSAGITMATAIASALSR
RPARMDIAMTGEVSLRGKVMPIGGVKEKLLAAHQAGIHKIVLPKDNEAQL
EELPKEVLEGLEIKLVEDVGEVLEYLLLPEPTMPPVV

>6wqh Chain S (length=11) Species: 44689 (Dictyostelium discoideum) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

AAAAAAAAAAA

Receptor-Ligand Complex Structure

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Structure summary

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PDB	6wqh Molecular basis for ATPase-powered substrate translocation by the Lon AAA+ protease.
Resolution	3.6 Å
Binding residue (original residue number in PDB)	Y397 I398
Binding residue (residue number reindexed from 1)	Y154 I155

Enzyme Commision number

3.4.21.53: endopeptidase La.

	Molecular Function
GO:0004176	ATP-dependent peptidase activity
GO:0004252	serine-type endopeptidase activity
GO:0005524	ATP binding
GO:0016887	ATP hydrolysis activity
GO:0043565	sequence-specific DNA binding

	Biological Process
GO:0006508	proteolysis
GO:0030163	protein catabolic process

PDB	RCSB:6wqh, PDBe:6wqh, PDBj:6wqh
PDBsum	6wqh
PubMed	34563541
UniProt	A0A059VAZ3

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Structure of PDB 6wqh Chain B Binding Site BS01