Structure of PDB 7krz Chain A

Receptor sequence

>7krzA (length=525) Species: 9606 (Homo sapiens)

IEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLT
SIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQG
KILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYV
GAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQN
ANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEK
LAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQV
EKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVM
GLAWTAMGGSTLFVETSLRRPQDKDGSLEVTGQLGEVMKESARIAYTFAR
AFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRP
VRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYD
LAAFITEGLEVHFVEHYREIFDIAF

3D structure

• PDB: 7krz Structures of the human LONP1 protease reveal regulatory steps involved in protease activation.
• Chain: A
• Resolution: 3.2 Å

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	peptide	A	T564 Y565 V566	T148 Y149 V150
BS02	ATP	A	H491 Y492 P525 V527 G528 K529 T530 S531 Y661 I669 V709 R710	H75 Y76 P109 V111 G112 K113 T114 S115 Y245 I253 V293 R294
BS03	BO2	A	A769 W770 T771 M810 K851 D852 G853 P854 S855 K898	A353 W354 T355 M388 K429 D430 G431 P432 S433 K476

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

External links

• PDB: RCSB:7krz, PDBe:7krz, PDBj:7krz
• PDBsum: 7krz
• PubMed: 34050165
• UniProt: P36776|LONM_HUMAN Lon protease homolog, mitochondrial (Gene Name=LONP1)