Structure of PDB 2nva Chain C

Receptor sequence
>2nvaC (length=367) Species: 10506 (Paramecium bursaria Chlorella virus 1) [Search protein sequence]
MNSVVNNILKAHPQTKSFYVSSPKIVEDLIDQWTILFPRVTPHYAVKCNN
DEVLLKTMCDKNVNFDCASSSEIKKVIQIGVSPSRIIFAHTMKTIDDLIF
AKDQGVDIATFDSSFELDKIHTYHPNCKMILRIRCDDPNATVQLGNKFGA
NEDEIRHLLEYAKQLDIEVIGISFHVGSGSRNPEAYYRAIKSSKEAFNEA
ISVGHKPYILDIGGGLHADIELSTMSDYINDAIKDFFPEDTVTIVAEPGR
FFAEHYSVLATQVIGKRVRDGLYEYFFNESTYGGFSNVIFEKSVPTPQLL
RDVPDDEEYVPSVLYGCTCDGVDVINHNVALPELHIGDWVYFPSWGAYTN
VLTTSFNGFGEYDVYYI
3D structure
PDB2nva X-ray Structure of Paramecium bursaria Chlorella Virus Arginine Decarboxylase: Insight into the Structural Basis for Substrate Specificity.
ChainC
Resolution1.8 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 E247
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 C D67 H176 S179 G215 G216 E252 G254 R255 E296 Y353 D66 H175 S178 G214 G215 E247 G249 R250 E291 Y348
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:2nva, PDBe:2nva, PDBj:2nva
PDBsum2nva
PubMed17305368
UniProtQ84527

[Back to BioLiP]