Structure of PDB 7krz Chain A Binding Site BS01

Receptor Information

>7krz Chain A (length=525) Species: 9606 (Homo sapiens)

IEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLT
SIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQG
KILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYV
GAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQN
ANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEK
LAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQV
EKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVM
GLAWTAMGGSTLFVETSLRRPQDKDGSLEVTGQLGEVMKESARIAYTFAR
AFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRP
VRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYD
LAAFITEGLEVHFVEHYREIFDIAF

Ligand information

>7krz Chain G (length=12) Species: 469008 (Escherichia coli BL21(DE3))

AAAAAAAAAAAA

Receptor-Ligand Complex Structure

Structure summary

• PDB: 7krz Structures of the human LONP1 protease reveal regulatory steps involved in protease activation.
• Resolution: 3.2 Å
• Binding residue (original residue number in PDB): T564 Y565 V566
• Binding residue (residue number reindexed from 1): T148 Y149 V150

Enzymatic activity

• Enzyme Commision number: 3.4.21.53: endopeptidase La.

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)