Structure of PDB 1kyi Chain Q

Receptor sequence
>1kyiQ (length=173) Species: 71421 (Haemophilus influenzae Rd KW20) [Search protein sequence]
TTIVSVRRNGQVVVGGDGQVSLGNTVMKGNARKVRRLYNGKVLAGFAGGT
ADAFTLFELFERKLEMHQGHLLKSAVELAKDWRTDRALRKLEAMLIVADE
KESLIITGIGDVVQPEEDQILAIGSGGNYALSAARALVENTELSAHEIVE
KSLRIAGDICVFTNTNFTIEELP
3D structure
PDB1kyi Crystal Structure of HslUV Complexed with a Vinyl Sulfone Inhibitor: Corroboration of a Proposed Mechanism of Allosteric Activation of HslV by HslU
ChainQ
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T1 K33 G45 S125
Catalytic site (residue number reindexed from 1) T1 K33 G45 S125
Enzyme Commision number 3.4.25.2: HslU--HslV peptidase.
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 LVS Q T1 V20 S21 M27 G49 T50 G124 S125 T1 V20 S21 M27 G49 T50 G124 S125
Gene Ontology
Molecular Function
GO:0004298 threonine-type endopeptidase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0030163 protein catabolic process
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005839 proteasome core complex
GO:0009376 HslUV protease complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1kyi, PDBe:1kyi, PDBj:1kyi
PDBsum1kyi
PubMed12054822
UniProtP43772|HSLV_HAEIN ATP-dependent protease subunit HslV (Gene Name=hslV)

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