Structure of PDB 2nva Chain D

Receptor sequence
>2nvaD (length=371) Species: 10506 (Paramecium bursaria Chlorella virus 1) [Search protein sequence]
MNSVVNNILKAHPHQTKSFYVSSPKIVEDLIDQWTILFPRVTPHYAVKCN
NDEVLLKTMCDKNVNFDCASSSEIKKVIQIGVSPSRIIFAHTMKTIDDLI
FAKDQGVDIATFDSSFELDKIHTYHPNCKMILRIRCDDPNATVQLGNKFG
ANEDEIRHLLEYAKQLDIEVIGISFHVGSGSRNPEAYYRAIKSSKEAFNE
AISVGHKPYILDIGGGLHADIDGELSTYMSDYINDAIKDFFPEDTVTIVA
EPGRFFAEHYSVLATQVIGKRVRDGLYEYFFNESTYGGFSNVIFEKSVPT
PQLLRDVPDDEEYVPSVLYGCTCDGVDVINHNVALPELHIGDWVYFPSWG
AYTNVLTTSFNGFGEYDVYYI
3D structure
PDB2nva X-ray Structure of Paramecium bursaria Chlorella Virus Arginine Decarboxylase: Insight into the Structural Basis for Substrate Specificity.
ChainD
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K48 H176 E252
Catalytic site (residue number reindexed from 1) K48 H176 E251
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 PL2 D C324 D325 C323 D324
BS02 PL2 D A46 K48 D67 H176 S179 G215 G216 E252 G254 R255 E296 Y353 A46 K48 D67 H176 S179 G215 G216 E251 G253 R254 E295 Y352
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004586 ornithine decarboxylase activity
Biological Process
GO:0006596 polyamine biosynthetic process
GO:0033387 putrescine biosynthetic process from ornithine
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2nva, PDBe:2nva, PDBj:2nva
PDBsum2nva
PubMed17305368
UniProtQ84527

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