Structure of PDB 6knk Chain B

Receptor sequence
>6knkB (length=383) Species: 158878 (Staphylococcus aureus subsp. aureus Mu50) [Search protein sequence]
MRIVQPVIEQLKAQSHPVCHYIYDLVGLEHHLQHITSSLPSNCQMYYAMA
ANSERTILDTISQYVEGFEVASQGEIAKGLAFKPANHIIFGGPGKTDEEL
RYAVSEGVQRIHVESMHELQRLNAILEDEDKTQHILLRVNLAGRPTQFGI
SEDEVDDVIEAALVMPNIHLDGFHFHSISNNLDSNLHVDVVKLYFKKAKS
WSEKHRFPLKHINLGGGIGVNYADLTSQFEWDNFVENFKTLIVEQEMEDV
TLNFECGRFIVAHIGYYVTEVLDIKKVHGAWYAILRGGTQQFRLPVSWQH
NHPFEIYRYKDNPYSFEKVSISRQDTTLVGQLCTPKDVFAREVQIDAIST
GDVIVFKYAGAYGWSISHHDFLSHPHPEFIYLT
3D structure
PDB6knk Structural Insights into Substrate Recognition and Activity Regulation of the Key Decarboxylase SbnH in Staphyloferrin B Biosynthesis.
ChainB
Resolution2.3 Å
3D
structure
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Enzymatic activity
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 DN9 B C344 T345 K347 C333 T334 K336
BS02 PO4 B G228 G268 R269 Y373 G217 G257 R258 Y362
BS03 X3J B R269 R304 S308 W309 Y373 I377 R258 R293 S297 W298 Y362 I366
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008836 diaminopimelate decarboxylase activity
GO:0016830 carbon-carbon lyase activity
Biological Process
GO:0006596 polyamine biosynthetic process
GO:0009089 lysine biosynthetic process via diaminopimelate

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Molecular Function
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Biological Process
External links
PDB RCSB:6knk, PDBe:6knk, PDBj:6knk
PDBsum6knk
PubMed31634470
UniProtA0A0H3JPF2

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