Structure of PDB 4usj Chain A

Receptor sequence
>4usjA (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.
ChainA
Resolution2.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K41 G44 G76 G77 R98 D196 D216 K255
Catalytic site (residue number reindexed from 1) K25 G28 G60 G61 R82 D180 D200 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 A K210 E284 I285 S287 E289 G290 G292 M294 K194 E268 I269 S271 E273 G274 G276 M278 PDBbind-CN: -logKd/Ki=4.00,IC50=0.1mM
BS02 ADP A G43 A45 T215 D216 V217 L221 A249 G251 M252 K255 G27 A29 T199 D200 V201 L205 A233 G235 M236 K239
BS03 NLG A G75 R98 N192 A195 G59 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4usj, PDBe:4usj, PDBj:4usj
PDBsum4usj
PubMed25416954
UniProtQ9SCL7|NAGK_ARATH Acetylglutamate kinase, chloroplastic (Gene Name=NAGK)

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