Structure of PDB 7ksm Chain F

Receptor sequence
>7ksmF (length=516) Species: 9606 (Homo sapiens) [Search protein sequence]
EKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSI
PWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKI
LCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGA
MPGKIIQCLKKTKTENPLILIDEVDKIPSSALLELLDPEQNANFLDHYLD
VPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLV
PQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAY
KIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGG
STLFVETSLRRPQDKDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPA
NDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTG
EVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGL
EVHFVEHYREIFDIAF
3D structure
PDB7ksm Structures of the human LONP1 protease reveal regulatory steps involved in protease activation.
ChainF
Resolution3.2 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 F H491 Y492 G526 V527 G528 K529 T530 S531 Y661 I669 Y673 V709 H73 Y74 G108 V109 G110 K111 T112 S113 Y236 I244 Y248 V284
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:7ksm, PDBe:7ksm, PDBj:7ksm
PDBsum7ksm
PubMed34050165
UniProtP36776|LONM_HUMAN Lon protease homolog, mitochondrial (Gene Name=LONP1)

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