Structure of PDB 2nva Chain G

Receptor sequence
>2nvaG (length=368) Species: 10506 (Paramecium bursaria Chlorella virus 1) [Search protein sequence]
MNSVVNNILKAHPQTKSFYVSSPKIVEDLIDQWTILFPRVTPHYAVKCNN
DEVLLKTMCDKNVNFDCASSSEIKKVIQIGVSPSRIIFAHTMKTIDDLIF
AKDQGVDIATFDSSFELDKIHTYHPNCKMILRIRCDDPNATVQLGNKFGA
NEDEIRHLLEYAKQLDIEVIGISFHVGSGSRNPEAYYRAIKSSKEAFNEA
ISVGHKPYILDIGGGLHADIDEGELSTMSDYINDAIDFFPETVTIVAEPG
RFFAEHYSVLATQVIGKRVRDGLYEYFFNESTYGGFSNVIFEKSVPTPQL
LRDVPDDEEYVPSVLYGCTCDGVDVINHNVALPELHIGDWVYFPSWGAYT
NVLTTSFNGFGEYDVYYI
3D structure
PDB2nva X-ray Structure of Paramecium bursaria Chlorella Virus Arginine Decarboxylase: Insight into the Structural Basis for Substrate Specificity.
ChainG
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) K47 H175 E248
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 G A46 K48 D67 H176 S179 G215 G216 E252 G254 R255 F295 E296 Y353 A45 K47 D66 H175 S178 G214 G215 E248 G250 R251 F291 E292 Y349
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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