BioLiP

Structure of PDB 1g3i Chain C

Receptor sequence

>1g3iC (length=319) Species: 727 (Haemophilus influenzae) [Search protein sequence]

SEMTPREIVSELDQHIIGQADAKRAVAIALRNRWRRMQLQEPLRHEVTPK
NILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVDSIIRDLTDSAM
KLVRQQEIAKNRAINPEELKQKAIDAVEQNGIVFIDEIDKICKKGADVSR
EGVQRDLLPLVEGSTVSTKHGMVKTDHILFIASGAFQVARPSDLIPELQG
RLPIRVELTALSAADFERILTEPHASLTEQYKALMATEGVNIAFTTDAVK
KIAEAAFRVNEKTENIGARRLHTVMERLMDKISFSASDMNGQTVNIDAAY
VADALGEVVENEDLSRFIL

3D structure

PDB

1g3i Crystal and solution structures of an HslUV protease-chaperone complex.

Chain

Resolution

3.41 Å

3D
structure

[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

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	ATP	C	I17 I18 G60 V61 G62 K63 T64 E65 D257 L336 I344 A393	I16 I17 G59 V60 G61 K62 T63 E64 D136 L211 I219 A268

Gene Ontology

	Molecular Function
GO:0005515	protein binding
GO:0005524	ATP binding
GO:0008233	peptidase activity
GO:0016887	ATP hydrolysis activity
GO:0036402	proteasome-activating activity

	Biological Process
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:0009376	HslUV protease complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

PDB	RCSB:1g3i, PDBe:1g3i, PDBj:1g3i
PDBsum	1g3i
PubMed	11106733
UniProt	P43773\|HSLU_HAEIN ATP-dependent protease ATPase subunit HslU (Gene Name=hslU)