Structure of PDB 7krz Chain E

Receptor sequence
>7krzE (length=517) Species: 9606 (Homo sapiens) [Search protein sequence]
FRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPW
GKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILC
FYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMP
GKIIQCLKKTKTENPLILIDEVDKIGRDPSSALLELLDPEQNANFLDHYL
DVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYL
VPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSA
YKIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMG
GSTLFVETSLRRPQDKDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAP
ANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMT
GEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEG
LEVHFVEHYREIFDIAF
3D structure
PDB7krz Structures of the human LONP1 protease reveal regulatory steps involved in protease activation.
ChainE
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 E Y492 G526 V527 G528 K529 T530 Y661 I669 Y673 V709 Q713 Y72 G106 V107 G108 K109 T110 Y237 I245 Y249 V285 Q289
BS02 BO2 E A769 W770 M810 K851 D852 G853 P854 S855 K898 A345 W346 M380 K421 D422 G423 P424 S425 K468
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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