Structure of PDB 3nzp Chain A

Receptor sequence
>3nzpA (length=583) Species: 192222 (Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819) [Search protein sequence]
MMDYGIDIWGNENFIIKNGKVCINYEKKPAIIDIVKELRDDGYKGPLLLR
FPHLIQKQIENIYGNFNKARKEFGYKGGFNAVYPLKVNQYPGFVKNLVKL
GKDYNYGLEAGSKAELLLAMAYNNEGAPITVNGFKDRELINIGFIAAEMG
HNITLTIEGLNELEAIIDIAKERFKPKPNIGLRVRLHSAKFGLTSTELIE
AVNLLKENKLLEQFTMIHFHLGSQITEIHPLKKALNEAGNIYTELRKMGA
KNLKAINLGGGLAVEYSQFKNEKSRNYTLREYANDVVFILKNIAEQKKDL
EPDIFIESGRFVAANHAVLIAPVLELFSQEYAENKLILKKQNPKLIDELY
DLYKSIKPSNALEYLHDSIDHLESILTLFDLGYVDLQDRSNAEILTHLIT
KKAILLLGEVQERYLVNFSLFQSMPDFWGLEQNFPIMPLDRLDEEPTRSA
SIWDITCDSDGEISYSKDKPLFLHDVDVEKENYFLGFFLVGAYQEVLGMK
HNLFTHPTEAIISINEKGYEVEGIIEAQSILDTLEDLDYDIHAIMDILNE
RISNSKLVNDKQKKHILGELYLFLNDNGYLKSI
3D structure
PDB3nzp Structures of bacterial biosynthetic arginine decarboxylases.
ChainA
Resolution3.0 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 A K86 H231 H233 S236 G273 E320 S321 G322 R323 Y519 K86 H218 H220 S223 G260 E307 S308 G309 R310 Y493
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:3nzp, PDBe:3nzp, PDBj:3nzp
PDBsum3nzp
PubMed21139196
UniProtQ0PAC6

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