Structure of PDB 6pxl Chain D

Receptor sequence
>6pxlD (length=401) Species: 562 (Escherichia coli) [Search protein sequence]
HSEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLNEELRHEVTP
KNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVKEVDSIIRDLT
DAAVKMVRVQAIEKNRYRAEELAEERILDVLIPPSAARQAFRKKLREGQL
DDKMGVEIMAPPGMEEMTSQLQSMFQNLKIKDAMKLLIEEEAAKLVNPEE
LKQDAIDAVEQHGIVFIDEIDKICKSGPDVSREGVQRDLLPLVEGCTVST
KHGMVKTDHILFIASGAFQIAKPSDLIPELQGRLPIRVELQALTTSDFER
ILTEPNASITVQYKALMATEGVNIEFTDSGIKRIAEAAWQVNESTENIGA
RRLHTVLERLMEEISYDASDLSGQNITIDADYVSKHLDALVADEDLSRFI
L
3D structure
PDB6pxl Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug.
ChainD
Resolution3.741 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 D I17 I18 T59 G60 V61 G62 K63 T64 E65 I343 A392 R393 I17 I18 T59 G60 V61 G62 K63 T64 E65 I301 A350 R351
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004176 ATP-dependent peptidase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008233 peptidase activity
GO:0016887 ATP hydrolysis activity
GO:0019904 protein domain specific binding
GO:0036402 proteasome-activating activity
GO:0042802 identical protein binding
Biological Process
GO:0006508 proteolysis
GO:0009408 response to heat
GO:0030164 protein denaturation
GO:0034605 cellular response to heat
GO:0043335 protein unfolding
GO:0051603 proteolysis involved in protein catabolic process
GO:1901800 positive regulation of proteasomal protein catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009376 HslUV protease complex
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6pxl, PDBe:6pxl, PDBj:6pxl
PDBsum6pxl
PubMed33472065
UniProtP0A6H5|HSLU_ECOLI ATP-dependent protease ATPase subunit HslU (Gene Name=hslU)

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