Structure of PDB 7ksm Chain B Binding Site BS01

Receptor Information
>7ksm Chain B (length=520) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIP
WGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKIL
CFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAM
PGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANF
LDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAI
AERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKV
LRKSAYKIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLA
WTAMGGSTLFVETSLRRPKDGSLEVTGQLGEVMKESARIAYTFARAFLMQ
HAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNL
AMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFI
TEGLEVHFVEHYREIFDIAF
Ligand information
>7ksm Chain G (length=12) Species: 469008 (Escherichia coli BL21(DE3)) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
AAAAAAAAAAAA
Receptor-Ligand Complex Structure
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PDB7ksm Structures of the human LONP1 protease reveal regulatory steps involved in protease activation.
Resolution3.2 Å
Binding residue
(original residue number in PDB)		Y565 V566 Y599
Binding residue
(residue number reindexed from 1)		Y146 V147 Y180
Enzymatic activity
Enzyme Commision number 3.4.21.53: endopeptidase La.
Gene Ontology
Molecular Function
GO:0004176 ATP-dependent peptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0006508 proteolysis
GO:0030163 protein catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7ksm, PDBe:7ksm, PDBj:7ksm
PDBsum7ksm
PubMed34050165
UniProtP36776|LONM_HUMAN Lon protease homolog, mitochondrial (Gene Name=LONP1)

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