Structure of PDB 2rd5 Chain B

Receptor sequence
>2rd5B (length=283) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
SPDYRVEILSESLPFIQKFRGKTIVVKYGGAAMTSPELKSSVVSDLVLLA
CVGLRPILVHGGGPDINRYLKQLNIPAEFRDGLRVTDATTMEIVSMVLVG
KVNKNLVSLINAAGATAVGLSGHDGRLLTARPVPNSAQLGFVGEVARVDP
SVLRPLVDYGYIPVIASVAADDSGQAYNINADTVAGELAAALGAEKLILL
TDVAGILENKEDPSSLIKEIDIKGVKKMIEDGKVAGGMIPKVKCCIRSLA
QGVKTASIIDGRRQHSLLHEIMSDEGAGTMITG
3D structure
PDB2rd5 Structural Basis for the Regulation of N-Acetylglutamate Kinase by PII in Arabidopsis thaliana.
ChainB
Resolution2.51 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) K27 G30 G63 D182 K241
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 K210 K232 E284 S287 E289 G292 M294 K196 K218 E270 S273 E275 G278 M280
BS02 ADP B A45 T215 D216 L221 K224 A249 G251 M252 K255 A31 T201 D202 L207 K210 A235 G237 M238 K241
BS03 NLG B G75 R98 N192 N194 A195 G61 R84 N178 N180 A181
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:2rd5, PDBe:2rd5, PDBj:2rd5
PDBsum2rd5
PubMed17913711
UniProtQ9SCL7|NAGK_ARATH Acetylglutamate kinase, chloroplastic (Gene Name=NAGK)

[Back to BioLiP]