Structure of PDB 1sio Chain C

Receptor sequence
>1sioC (length=352) Species: 192387 (Alicyclobacillus sendaiensis) [Search protein sequence]
TAYTPLDVAQAYQFPEGLDGQGQCIAIIELGGGYDEASLAQYFASLGVPA
PQVVSVSVDGASNQPTGDPSGPDGEVELDIEVAGALAPGAKFAVYFAPNT
DAGFLDAITTAIHDPTLKPSVVSISWGGPEDSWTSAAIAAMNRAFLDAAA
LGVTVLAAAGDSGSTDGEQDGLYHVDFPAASPYVLACGGTRLVASGGRIA
QETVWNDGPDGGATGGGVSRIFPLPAWQEHANVPPSANPGASSGRGVPDL
AGNADPATGYEVVIDGEATVIGGTSAVAPLFAALVARINQKLGKAVGYLN
PTLYQLPADVFHDITEGNNDIANRAQIYQAGPGWDPCTGLGSPIGVRLLQ
AL
3D structure
PDB1sio Crystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activity
ChainC
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E78 D82 D164 S278
Catalytic site (residue number reindexed from 1) E75 D79 D161 S275
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 peptide C E78 N102 S128 W129 G130 D164 D179 G276 S278 E75 N99 S125 W126 G127 D161 D176 G273 S275
BS02 CA C D316 I317 G334 G336 D338 D313 I314 G331 G333 D335
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1sio, PDBe:1sio, PDBj:1sio
PDBsum1sio
PubMed15014068
UniProtQ8GB88

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