Structure of PDB 7sxo Chain C

Receptor sequence
>7sxoC (length=487) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
EQYSIPRAKKILDEDHYGMVDVKDRILEFIAVGKLLGKVDGKIICFVGPP
GVGKTSIGKSIARALNRKFFRFSVGGMTDVAEIKGHRRTYIGALPGRVVQ
ALKKCQTQNPLILIDEIDKIIHGDPSAALLEVLDPEQNNSFLDNYLDIPI
DLSKVLFVCTANSLETIPRPLLDRMEVIELTGYVAEDKVKIAEQYLVPSA
KKSAGLENSHVDMTEDAITALMKYYCRESGVRNLKKHIEKIYRKAALQVV
KKLSKINVSISQKNLKDYVGPPVYTTDRLYETTPPGVVMGLAWTNMGGCS
LYVESVLEQPLHNCKHPTFERTGQLGDVMKESSRLAYSFAKMYLAQKFPE
NRFFEKASIHLHCPEGATPKDGPSAGVTMATSFLSLALNKSIDPTVAMTG
ELTLTGKVLRIGGLREKAVAAKRSGAKTIIFPKDNLNDWEELPDNVKEGL
EPLAADWYNDIFQKLFKDVNTKEGNSVWKAEFEILDA
3D structure
PDB7sxo Cryo-EM structure of hexameric yeast Lon protease (PIM1) highlights the importance of conserved structural elements.
ChainC
Resolution3.3 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 C H600 P634 G635 V636 G637 K638 T639 Y783 V819 R820 H16 P50 G51 V52 G53 K54 T55 Y195 V231 R232
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:0006515 protein quality control for misfolded or incompletely synthesized proteins
GO:0030163 protein catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7sxo, PDBe:7sxo, PDBj:7sxo
PDBsum7sxo
PubMed35143841
UniProtP36775|LONM_YEAST Lon protease homolog, mitochondrial (Gene Name=PIM1)

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