Structure of PDB 1do2 Chain C

Receptor sequence
>1do2C (length=407) Species: 562 (Escherichia coli) [Search protein sequence]
SEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLNEELRHEVTPK
NILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIR
DLTDAAVKMVRVQAIEKNRYRAEELAEERILDVLIPPAKNNWGQTEQQQE
PSAARQAFRKKLREGQLDDKEIEKQKARKLKIKDAMKLLIEEEAAKLVNP
EELKQDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVE
GCTVSTKHGMVKTDHILFIASGAFQIAKPSDLIPELQGRLPIRVELQALT
TSDFERILTEPNASITVQYKALMATEGVNIEFTDSGIKRIAEAAWQVNES
TENIGARRLHTVLERLMEEISYDASDLSGQNITIDADYVSKHLDALVADE
DLSRFIL
3D structure
PDB1do2 The structures of HsIU and the ATP-dependent protease HsIU-HsIV.
ChainC
Resolution4.0 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 ANP C H16 I17 I18 P58 T59 G60 V61 G62 K63 T64 E65 L335 A392 R393 H15 I16 I17 P57 T58 G59 V60 G61 K62 T63 E64 L299 A356 R357
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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Cellular Component
External links
PDB RCSB:1do2, PDBe:1do2, PDBj:1do2
PDBsum1do2
PubMed10693812
UniProtP0A6H5|HSLU_ECOLI ATP-dependent protease ATPase subunit HslU (Gene Name=hslU)

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