Structure of PDB 3n29 Chain A

Receptor sequence
>3n29A (length=371) Species: 407148 (Campylobacter jejuni subsp. jejuni 81116) [Search protein sequence]
FYEKIQTPAYILEEDKLRKNCELLASVGEKSGAKVLLALKGFAFSGAMKI
VGEYLKGCTCSGLWEAKFAKEYMDKEIHTYSPAFKEDEIGEIASLSHHIV
FNSLAQFHKFQSKTQKNSLGLRCNVEFSGRYSRLGIRAKDFENVDLNAIE
GLHFHALCEESADALEAVLKVFEEKFGKWIGQMKWVNFGGGHHITKKGYD
VEKLIALCKNFSDKYGVQVYLEPGEAVGWQTGNLVASVVDIIENEKQIAI
LDTSSEAHMPDTIIMPYTSEVLNARILATRENEKISDLKENEFAYLLTGN
TCLAGDVMGEYAFDKKLKIGDKIVFLDQIHYTIVKNTTFNGIRLPNLMLL
DHKNELQMIREFSYKDYSLRN
3D structure
PDB3n29 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.
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.1.1.96: carboxynorspermidine 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 A A39 K41 H166 G201 G202 E233 G235 E236 Y342 A38 K40 H155 G190 G191 E222 G224 E225 Y331
BS02 NSD A C169 E236 D272 Y342 K346 C158 E225 D261 Y331 K335
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008836 diaminopimelate decarboxylase activity
GO:0016830 carbon-carbon lyase activity
GO:0016831 carboxy-lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0008295 spermidine biosynthetic process
GO:0009089 lysine biosynthetic process via diaminopimelate
GO:0045312 nor-spermidine biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:3n29, PDBe:3n29, PDBj:3n29
PDBsum3n29
PubMed20534592
UniProtA8FNH9|NSPC_CAMJ8 Carboxynorspermidine/carboxyspermidine decarboxylase (Gene Name=nspC)

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