Structure of PDB 1c9j Chain A

Receptor sequence
>1c9jA (length=269) Species: 1467 (Lederbergia lenta) [Search protein sequence]
AQSVPWGISRVQAPAAHNRGLTGSGVRVAVLDTGISTHPDLNIRGGASFV
PGEPSTQDGNGHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGASGSG
SYSSIAQGLEWAGNNGMHVASLSLGSPSPSATLEQAVNSATSRGVLVVAA
SGNSGAGSISYPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQ
STYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQIRNHLKNTATS
LGSTNLYGSGLVNAEAAAR
3D structure
PDB1c9j Engineered Bacillus lentus subtilisins having altered flexibility.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) D32 H64 N155 S221
Catalytic site (residue number reindexed from 1) D32 H62 N153 S215
Enzyme Commision number 3.4.21.62: subtilisin.
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 CA A Q2 D41 L75 N77 I79 V81 Q2 D40 L73 N75 I77 V79
BS02 CA A A169 R170 Y171 A174 G195 A163 R164 Y165 A168 G189
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0030435 sporulation resulting in formation of a cellular spore
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1c9j, PDBe:1c9j, PDBj:1c9j
PDBsum1c9j
PubMed10493860
UniProtP29600|SUBS_LEDLE Subtilisin Savinase

[Back to BioLiP]