Structure of PDB 4ypl Chain A

Receptor sequence
>4yplA (length=537) Species: 172827 (Meiothermus taiwanensis) [Search protein sequence]
SDLEALRKKIEEVGMPEAVKTKALKELDRLERMQQGSPEATVARTYLDWL
TEVPWSKADPEVLDINHTRQVLDEDHYGLKDVKERILEYLAVRQLTQGLD
VRNKAPILVLVGPPGVGKTSLGRSIARSMNRKFHRISLGGVRDEAEIRGH
RRTYIGAMPGKLIHAMKQVGVINPVILLDQIDKMSSDWRGDPASAMLEVL
DPEQNNTFTDHYLDVPYDLSKVFFITTANTLQTIPRPLLDRMEVIEIPGY
TNMEKQAIARQYLWPKQVRESGMEGRIEVTDAAILRVISEYTREAGVRGL
ERELGKIARKGAKFWLEGAWEGLRTIDASDIPTYLGIPRYRPDKAETEPQ
VGTAQGLAWTPVGGTLLTIEVAAVPGSGKLSLTGQLGEVMKESAQAALTY
LRAHTQDYGLPEDFYNKVDLHVHVPDGATPKDGPSAGITMATAIASALSR
RPARMDIAMTGEVSLRGKVMPIGGVKEKLLAAHQAGIHKIVLPKDNEAQL
EELPKEVLEGLEIKLVEDVGEVLEYLLLPEPTMPPVV
3D structure
PDB4ypl Structural Insights into the Allosteric Operation of the Lon AAA+ Protease
ChainA
Resolution3.45 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 4KZ A A601 W602 L610 M633 K674 D675 G676 P677 S678 K721 A358 W359 L367 M390 K431 D432 G433 P434 S435 K478
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:4ypl, PDBe:4ypl, PDBj:4ypl
PDBsum4ypl
PubMed27041592
UniProtA0A059VAZ3

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