Structure of PDB 4usj Chain B

Receptor sequence
>4usjB (length=281) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
DYRVEILSESLPFIQKFRGKTIVVKYGGAAMTSPELKSSVVSDLVLLACV
GLRPILVHGGGPDINRYLKQLNIPAEFRDGLRVTDATTMEIVSMVLVGKV
NKNLVSLINAAGATAVGLSGHDGRLLTARPVPNSAQLGFVGEVARVDPSV
LRPLVDYGYIPVIASVAADDSGQAYNINADTVAGELAAALGAEKLILLTD
VAGILENKEDPSSLIKEIDIKGVKKMIEDGKVAGGMIPKVKCCIRSLAQG
VKTASIIDGRRQHSLLHEIMSDEGAGTMITG
3D structure
PDB4usj A Widespread Glutamine-Sensing Mechanism in the Plant Kingdom.
ChainB
Resolution2.85 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) K41 G44 G77 D196 K255
Catalytic site (residue number reindexed from 1) K25 G28 G61 D180 K239
Enzyme Commision number 2.7.2.8: acetylglutamate kinase.
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 ARG B F33 K210 K232 E284 I285 S287 E289 G290 M294 F17 K194 K216 E268 I269 S271 E273 G274 M278 PDBbind-CN: -logKd/Ki=4.00,IC50=0.1mM
BS02 X2W B G75 G76 G77 R98 N192 A195 G59 G60 G61 R82 N176 A179
Gene Ontology
Molecular Function
GO:0003991 acetylglutamate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
Biological Process
GO:0006526 L-arginine biosynthetic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:4usj, PDBe:4usj, PDBj:4usj
PDBsum4usj
PubMed25416954
UniProtQ9SCL7|NAGK_ARATH Acetylglutamate kinase, chloroplastic (Gene Name=NAGK)

[Back to BioLiP]