Structure of PDB 7ksl Chain B

Receptor sequence
>7kslB (length=520) Species: 9606 (Homo sapiens) [Search protein sequence]
FRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPW
GKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILC
FYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMP
GKIIQCLKKTKTENPLILIDEVDKIPSSALLELLDPEQNANFLDHYLDVP
VDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQ
ARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKI
VSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGST
LFVETSLRRPQDKDAKGDKDGSLEVTGQLGEVMKESARIAYTFARAFLMQ
HAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNL
AMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFI
TEGLEVHFVEHYREIFDIAF
3D structure
PDB7ksl Structures of the human LONP1 protease reveal regulatory steps involved in protease activation.
ChainB
Resolution3.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.21.53: endopeptidase La.
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 ADP B Y492 G526 V527 G528 K529 S531 Y661 I669 Y673 Q677 R710 Y72 G106 V107 G108 K109 S111 Y234 I242 Y246 Q250 R283
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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7ksl, PDBe:7ksl, PDBj:7ksl
PDBsum7ksl
PubMed34050165
UniProtP36776|LONM_HUMAN Lon protease homolog, mitochondrial (Gene Name=LONP1)

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