Structure of PDB 7krz Chain D

Receptor sequence
>7krzD (length=520) Species: 9606 (Homo sapiens) [Search protein sequence]
DAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDW
LTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGST
QGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRT
YVGAMPGKIIQCLKKTKTENPLILIDEVDKIGPSSALLELLDPEQNANFL
DHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIA
ERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVL
RKSAYKIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAW
TAMGGSTLFVETSLRRPQKDGSLEVTGQLGEVMKESARIAYTFARAFLMQ
HAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNL
AMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFI
TEGLEVHFVEHYREIFDIAF
3D structure
PDB7krz Structures of the human LONP1 protease reveal regulatory steps involved in protease activation.
ChainD
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 ATP D E614 R652 E194 R232
BS02 ATP D H491 Y492 G526 V527 G528 K529 T530 S531 Y661 I669 R710 H77 Y78 G112 V113 G114 K115 T116 S117 Y241 I249 R290
BS03 BO2 D A769 W770 T771 L778 M810 K851 D852 G853 P854 S855 A349 W350 T351 L358 M383 K424 D425 G426 P427 S428
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
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Biological Process
External links
PDB RCSB:7krz, PDBe:7krz, PDBj:7krz
PDBsum7krz
PubMed34050165
UniProtP36776|LONM_HUMAN Lon protease homolog, mitochondrial (Gene Name=LONP1)

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