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
PDB1g3i Crystal and solution structures of an HslUV protease-chaperone complex.
ChainC
Resolution3.41 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
External links
PDB RCSB:1g3i, PDBe:1g3i, PDBj:1g3i
PDBsum1g3i
PubMed11106733
UniProtP43773|HSLU_HAEIN ATP-dependent protease ATPase subunit HslU (Gene Name=hslU)

[Back to BioLiP]