Structure of PDB 3hjr Chain A

Receptor sequence
>3hjrA (length=593) Species: 646 (Aeromonas sobria) [Search protein sequence]
GCAPLTGKESGMDIGRSSTERCLPGANPLQDQQWYLLNSGQDGFSARGGI
AGNDLNLWWAHRTGVLGQGVNVAVVDDGLAIAHPDLADNVRPGSKNVVTG
SDDPTPTDPDTAHGTSVSGIIAAVDNAIGTKGIAPRAQLQGFNLLDDNSQ
QLQKDWLYALGDSNASRDNRVFNQSYGMSVVDPRSANSLDQSQLDRLFEQ
QTLKAQGAAYIKAAGNGFNKIAAGGYVLNRTGNGPKLPFENSNLDPSNSN
FWNLVVSALNADGVRSSYSSVGSNIFLSATGGEYGTDTPAMVTTDLPGCD
MGYNRTDDPSTNRLHGNSQLDASCDYNGVMNGTSSATPSTSGAMALLMSA
YPDLSVRDLRDLLARSATRVDAKHQPVMVSYTSSTGKVRDVKGLEGWERN
AAGMWFSPTYGFGLIDVNKALELAANHQPLPPLVQLPWQKINVTGSAAAI
ADVGNSPTSSTTRIATPLTVEAVQVMVSLDHQRLPDLLIELVSPAGTRSI
LLSPFNSLVGQSLDQQQLGFVRTKGLRDMRMLSNKFYGESAQGTWRLEVT
DVANGTRQVSLLNRETRERTTLTERNNRQPGKLISWSLRVLGH
3D structure
PDB3hjr Structural basis for the kexin-like serine protease from Aeromonas sobria as a sepsis-causing factor
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D78 H115 N218 S336
Catalytic site (residue number reindexed from 1) D76 H113 N216 S334
Enzyme Commision number 3.4.21.121: Lys-Lys/Arg-Xaa endopeptidase.
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 N29 D87 V126 N128 I130 T132 N27 D85 V124 N126 I128 T130
BS02 CA A D454 D488 D553 A555 N578 N579 D452 D486 D551 A553 N576 N577
BS03 CA A D297 L298 G300 M303 N306 C326 D295 L296 G298 M301 N304 C324
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
Cellular Component
GO:0005576 extracellular region
GO:0042597 periplasmic space

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3hjr, PDBe:3hjr, PDBj:3hjr
PDBsum3hjr
PubMed19654332
UniProtQ9L5A4|ASP_AERSO Aeromonas extracellular serine protease (Gene Name=asp)

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