Structure of PDB 3n2o Chain D

Receptor sequence
>3n2oD (length=629) Species: 196600 (Vibrio vulnificus YJ016) [Search protein sequence]
LDRVRADYNVHYWSQGFYGIDDQGEMYVSPRSDNAHQIQLSKIVKQLEER
QLNVPVLVRFPQILHQRVHSICDAFNQAIEEYQYPNKYLLVYPIKVNQQR
EVVDEILASQAQLETKQLGLEAGSKPELLAVLAMAQHASSVIVCNGYKDR
EYIRLALIGEKLGHKVFIVLEKMSELDLVLREAKSLGVTPRLGIRIRLAS
QGAGKWQASGGEKSKFGLSASQVLNVISRLKKENQLDTLQLVHFHLGSQM
ANIRDVRNGVNESARFYCELRTLGANITYFDVGGGLAIDYDGTRSQSSNS
MNYGLVEYARNIVNTVGDVCKDYKQPMPVIISESGRSLTAHHAVLISNVI
GTETYKPETVTEPEEDFPLLLNNMWRSWLNLHNGTDARALIEIYNDTQSD
LAEVHSQFATGVLTLEHRAWAEQTSLRIYYELNRLMSTKNRFHRPILDEL
SERLADKFFVNFSLFQSLPDSWGIDQVFPVLPLSGLQNAADRRAVMLDIT
CDSDGAIDAYVDGQGIESTLPVPAWNEDEPYLMGFFLVGAYQEILGDMHN
LFGDTHSVVVNVGDQGEINIDFINEGDTVEDMMRYVHIDVDQIRKNYHSL
VSQRVDQEEQQQILAELEQGLSGYTYLED
3D structure
PDB3n2o Evolution of substrate specificity within a diverse family of beta/alpha-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine.
ChainD
Resolution2.3 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.19: arginine 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 PLP D P103 K105 H255 S258 G294 G295 E343 G345 Y551 P93 K95 H245 S248 G284 G285 E333 G335 Y541
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008792 arginine decarboxylase activity
GO:0016831 carboxy-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006527 arginine catabolic process
GO:0008295 spermidine biosynthetic process
GO:0033388 putrescine biosynthetic process from arginine

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3n2o, PDBe:3n2o, PDBj:3n2o
PDBsum3n2o
PubMed20534592
UniProtQ7MK24|SPEA_VIBVY Biosynthetic arginine decarboxylase (Gene Name=speA)

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