Structure of PDB 1yyf Chain B

Receptor sequence
>1yyfB (length=408) Species: 562 (Escherichia coli) [Search protein sequence]
MSEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLNEELRHEVTP
KNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSII
RDLTDAAVKMVRVQAIEKNRYRAEELAEERILDVLIPPAKNNWGQTEQQQ
EPSAARQAFRKKLREGQLDDKEIEKQKARKLKIKDAMKLLIEEEAAKLVN
PEELKQDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLV
EGCTVSTKHGMVKTDHILFIASGAFQIAKPSDLIPELQGRLPIRVELQAL
TTSDFERILTEPNASITVQYKALMATEGVNIEFTDSGIKRIAEAAWQVNE
STENIGARRLHTVLERLMEEISYDASDLSGQNITIDADYVSKHLDALVAD
EDLSRFIL
3D structure
PDB1yyf Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects.
ChainB
Resolution4.16 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 B I17 I18 G60 V61 G62 K63 T64 E65 L335 I343 A392 R393 I17 I18 G60 V61 G62 K63 T64 E65 L300 I308 A357 R358
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:1yyf, PDBe:1yyf, PDBj:1yyf
PDBsum1yyf
PubMed15983416
UniProtP0A6H5|HSLU_ECOLI ATP-dependent protease ATPase subunit HslU (Gene Name=hslU)

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