Structure of PDB 1sio Chain B

Receptor sequence
>1sioB (length=355) Species: 192387 (Alicyclobacillus sendaiensis) [Search protein sequence]
APTAYTPLDVAQAYQFPEGLDGQGQCIAIIELGGGYDEASLAQYFASLGV
PAPQVVSVSVDGASNQPTGDPSGPDGEVELDIEVAGALAPGAKFAVYFAP
NTDAGFLDAITTAIHDPTLKPSVVSISWGGPEDSWTSAAIAAMNRAFLDA
AALGVTVLAAAGDSGSTDGEQDGLYHVDFPAASPYVLACGGTRLVASGGR
IAQETVWNDGPDGGATGGGVSRIFPLPAWQEHANVPPSANPGASSGRGVP
DLAGNADPATGYEVVIDGEATVIGGTSAVAPLFAALVARINQKLGKAVGY
LNPTLYQLPADVFHDITEGNNDIANRAQIYQAGPGWDPCTGLGSPIGVRL
LQALL
3D structure
PDB1sio Crystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activity
ChainB
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) E77 D81 D163 S277
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 B E78 N102 S128 W129 G130 G163 D164 D179 G276 T277 S278 E77 N101 S127 W128 G129 G162 D163 D178 G275 T276 S277
BS02 CA B D316 I317 G334 G336 D338 D315 I316 G333 G335 D337
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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