Structure of PDB 8d5r Chain A

Receptor sequence
>8d5rA (length=461) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium) [Search protein sequence]
MTDSIMQNYNQLREQVINGDRRFQHKDGHLCFEGVDLDALARQYPTPFYV
FSEPEIIRNIHEIQQAFAAHKNTKTFFASKTCSVMGVLKAIRDAGICAEA
NSQYEVRKCLEIGFRGDQIVFNGVVKKPADLEYAIANDLYLINVDSLYEL
EHIDAISRKLKKVANVCVRVEPNVVTAFHAKSGLDLEQAEETCRRILAMP
YVHLRGLHMHVGDQVPESEPFAKATKVLVDESRRLEEVLGIKFDLINVGG
GIPVPYKYDDENGDPLKDNMYAGITAQDFADAVIREVHKWRTDVEICIEP
GRKVTGSAAVLLTEVSCEKRKTNYDLNGNVECHVEWKFVDAGYSVLSDSQ
HFDWFFYVYNASRMTAAHDAWIKLAGPLCDGGDYFHMGVKGEEFLLPKET
HVGDIVAFLDAGAYTIESQTVFNNRPRTGVVMIDKNGDTRLIRREDSYED
MVKYDIYLAAA
3D structure
PDB8d5r The Y430F mutant of Salmonella d-ornithine/d-lysine decarboxylase has altered stereospecificity and a putrescine allosteric activation site.
ChainA
Resolution1.44 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.116: D-ornithine/D-lysine decarboxylase.
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 ORX A A78 K80 H218 D221 G259 E307 G309 R310 Y422 A78 K80 H210 D213 G251 E299 G301 R302 Y414
BS02 PUT A Q358 H359 D361 Q350 H351 D353
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008836 diaminopimelate decarboxylase activity
GO:0016830 carbon-carbon lyase activity
GO:0016831 carboxy-lyase activity
Biological Process
GO:0009089 lysine biosynthetic process via diaminopimelate

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Molecular Function
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Biological Process
External links
PDB RCSB:8d5r, PDBe:8d5r, PDBj:8d5r
PDBsum8d5r
PubMed36265649
UniProtQ8ZNC4|DOKDC_SALTY D-ornithine/D-lysine decarboxylase (Gene Name=dokD)

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