Structure of PDB 2nv9 Chain E

Receptor sequence
>2nv9E (length=370) Species: 10506 (Paramecium bursaria Chlorella virus 1) [Search protein sequence]
MNSVVNNILKAHPQTKSFYVSSPKIVEDLIDQWTILFPRVTPHYAVKCNN
DEVLLKTMCDKNVNFDCASSSEIKKVIQIGVSPSRIIFAHTMKTIDDLIF
AKDQGVDIATFDSSFELDKIHTYHPNCKMILRIRCDDPNAAVQLGNKFGA
NEDEIRHLLEYAKQLDIEVIGISFHVGSGSRNPEAYYRAIKSSKEAFNEA
ISVGHKPYILDIGGGLHADIDEGELSTMSDYINDAIKDFFPEDTVTIVAE
PGRFFAEHYSVLATQVIGKRVRDGLYEYFFNESTYGGFSNVIFEKSVPTP
QLLRDVPDDEEYVPSVLYGCTCDGVDVINHNVALPELHIGDWVYFPSWGA
YTNVLTTSFNGFGEYDVYYI
3D structure
PDB2nv9 X-ray Structure of Paramecium bursaria Chlorella Virus Arginine Decarboxylase: Insight into the Structural Basis for Substrate Specificity.
ChainE
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) K48 H176 E252
Catalytic site (residue number reindexed from 1) K47 H175 E250
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 E K48 D67 H176 S179 G215 G216 E252 G254 R255 Y353 K47 D66 H175 S178 G214 G215 E250 G252 R253 Y351
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2nv9, PDBe:2nv9, PDBj:2nv9
PDBsum2nv9
PubMed17305368
UniProtQ84527

[Back to BioLiP]