Structure of PDB 4kzt Chain A

Receptor sequence
>4kztA (length=431) Species: 394221 (Maricaulis maris MCS10) [Search protein sequence]
RQTIVQLLSHMRDGKEIREYLHRFSGIDQERFAVIKVGGAVIQDDLPGLA
SALAFLQTVGLTPVVVHGGGPQLDAALEAADIPTERVDGLRVTRDEAMPI
IRDTLTQANLALVDAIRDAGGRAAAVPRGVFEADIVDADKLGRVGEPRHI
HLDLVGSAARAGQAAILACLGETPDGTLVNINADVAVRALVHALQPYKVV
FLTGTGGLLDEDGDILSSINLATDFGDLMQADWVNGGMRLKLEEIKRLLD
DLPLSSSVSITRPSELARELFTHAGSGTLIRRGERMVATDDKSSLDLGRL
DNLVKAAFGRPAVEGYWDRLRVDRAFVTESYRAAAITTRLDGWVYLDKFA
VLDDARGEGLGRTVWNRMVDYAPQLIWRSRTNNPVNGFYFEECDGAVRRD
EWTVFWRGEMGPVEVADVVEKAFALPPTLEA
3D structure
PDB4kzt Structure of N-acetyl-L-glutamate synthase/kinase from Maricaulis maris with the allosteric inhibitor L-arginine bound.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K44 G47 G78 D192 K249
Catalytic site (residue number reindexed from 1) K36 G39 G70 D184 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 A Y28 K206 S225 E277 L278 T280 G285 T286 L287 Y20 K198 S217 E269 L270 T272 G277 T278 L279
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003991 acetylglutamate kinase activity
GO:0004042 L-glutamate N-acetyltransferase activity
GO:0016301 kinase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0006526 L-arginine biosynthetic process
GO:0016310 phosphorylation
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:4kzt, PDBe:4kzt, PDBj:4kzt
PDBsum4kzt
PubMed23850694
UniProtQ0ASS9

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