Structure of PDB 3m6a Chain E

Receptor sequence
>3m6aE (length=496) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
TGEVQTLTEKIEEAGMPDHVKETALKELNRYEKIPSSSAESSVIRNYIDW
LVALPWTDETDDKLDLKEAGRLLDEEHHGLEKVKERILEYLAVQKLTKSL
KGPILCLAGPPGVGKTSLAKSIAKSLGRKFVRISLGGRIIQGMKKAGKLN
PVFLLDEIDKMSAMLEVLDPEQNSSFSDHYIEETFDLSKVLFIATANNLA
TIPGPLRDRMEIINIAGYTEIEKLEIVKDHLLPKQIKEHGLKKSNLQLRD
QAILDIIRYYTREAGVRSLERQLAAICRKAAKAIVAEERKRITVTEKNLQ
DFIGKRIFRYGQAETEDQVGVVTGLAYTTVGGDTLSIEVSLSPGKGKLIL
TGKLGDVMRESAQAAFSYVRSKTEELGIEPDFHEKYDIHIHVPEGAVPKD
GPAAGITMATALVSALTGRAVSREVGMTGEITLRGRVLPIGGLKEKALGA
HRAGLTTIIAPKDNEKDIEDIPESVREGLTFILASHLDEVLEHALV
3D structure
PDB3m6a Crystal Structures of Bacillus subtilis Lon Protease.
ChainE
Resolution3.4 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 3.4.21.53: endopeptidase La.
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 E H322 G357 V358 G359 K360 T361 S362 Y492 I500 V540 H77 G112 V113 G114 K115 T116 S117 Y218 I226 V266
Gene Ontology
Molecular Function
GO:0004176 ATP-dependent peptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0006508 proteolysis
GO:0030163 protein catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3m6a, PDBe:3m6a, PDBj:3m6a
PDBsum3m6a
PubMed20600124
UniProtP37945|LON1_BACSU Lon protease 1 (Gene Name=lon1)

[Back to BioLiP]