Structure of PDB 5arb Chain A

Receptor sequence
>5arbA (length=269) Species: 1467 (Lederbergia lenta) [Search protein sequence]
AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFV
PGEPSTQDGNGHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGASGSG
SVSSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAA
SGNSGAGSISYPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQ
STYPGSTYASCNGTSMATPHVAGAAALVKQKNPSWSNVQIRNHLKNTATS
LGSTNLYGSGLVNAEAATR
3D structure
PDB5arb Cooperative Bio-Metallic Selectivity in a Tailored Protease Enables Creation of a C-C Cross-Coupling Heckase
ChainA
Resolution1.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 EI3 A Y209 A215 S216 C217 Y203 A209 S210 C211
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:5arb, PDBe:5arb, PDBj:5arb
PDBsum5arb
PubMed
UniProtP29600|SUBS_LEDLE Subtilisin Savinase

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