Structure of PDB 5txv Chain D

Receptor sequence
>5txvD (length=333) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
SEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLNEELRHEVTPK
NILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEGKEVDSIIRDLTD
AAVKMVRVQAIEKNRYRAEELAKLLIEEEAAKLVNPEELKQDAIDAVEQH
GIVFIDEIDKICKSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILF
IASGAFQIAKPSDLIPELQGRLPIRVELQALTTSDFERILTEPNASITVQ
YKALMATEGVNIEFTDSGIKRIAEAAWQVNESTENIGARRLHTVLERLME
EISYDASDLSGQNITIDADYVSKHLDALVADED
3D structure
PDB5txv Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation.
ChainD
Resolution7.086 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 G62 K63 T64 E65 R393 I16 I17 T58 G59 G61 K62 T63 E64 R289
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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Cellular Component
External links
PDB RCSB:5txv, PDBe:5txv, PDBj:5txv
PDBsum5txv
PubMed28223361
UniProtP0A6H5|HSLU_ECOLI ATP-dependent protease ATPase subunit HslU (Gene Name=hslU)

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