Structure of PDB 7krz Chain F

Receptor sequence
>7krzF (length=512) Species: 9606 (Homo sapiens) [Search protein sequence]
KFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIP
WGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKIL
CFYGPPGVGKTSIARSIARALNREYFRFSVGAEIKGHRRTYVGAMPGKII
QCLKKTKTENPLILIDEVDKIGDPSSALLELLDPEQNANFLDHYLDVPVD
LSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQAR
ALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVS
GEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLF
VETSLRRPQDKDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPANDYL
VTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSL
TGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHF
VEHYREIFDIAF
3D structure
PDB7krz 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 V527 G528 K529 T530 I669 Y673 V709 H72 Y73 V108 G109 K110 T111 I240 Y244 V280
BS02 BO2 F A769 W770 M810 K851 D852 G853 P854 S855 K898 A340 W341 M375 K416 D417 G418 P419 S420 K463
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:7krz, PDBe:7krz, PDBj:7krz
PDBsum7krz
PubMed34050165
UniProtP36776|LONM_HUMAN Lon protease homolog, mitochondrial (Gene Name=LONP1)

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