Structure of PDB 2j0w Chain A

Receptor sequence
>2j0wA (length=447) Species: 562 (Escherichia coli) [Search protein sequence]
EIVVSKFGGTSVADFDAMNRSADIVLSDANVRLVVLSASAGITNLLVALA
EGLEPGERFEKLDAIRNIQFAILERLRYPNVIREEIERLLENITVLAEAA
ALATSPALTDELVSHGELMSTLLFVEILRERDVQAQWFDVRKVMRTNDRF
GRAEPDIAALAELAALQLLPRLNEGLVITQGFIGSENKGRTTTLGRGGSD
YTAALLAEALHASRVDIWTDVPGIYTTDPRVVSAAKRIDEIAFAEAAEMA
TFGAKVLHPATLLPAVRSDIPVFVGSSKDPRAGGTLVCNKTENPPLFRAL
ALRRNQTLLTLHSLNMLHSRGFLAEVFGILARHNISVDLITTSEVSVALT
LDTTGSTSTGDTLLTQSLLMELSALCRVEVEEGLALVALIGNDLSKACGV
GKEVFGVLEPFNIRMICYGASSHNLCFLVPGEDAEQVVQKLHSNLFE
3D structure
PDB2j0w Structures of R- and T-State Escherichia Coli Aspartokinase III: Mechanisms of the Allosteric Transition and Inhibition by Lysine.
ChainA
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.2.4: aspartate 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 ASP A S39 T45 E119 F184 R198 G199 S201 S37 T43 E117 F182 R196 G197 S199
BS02 ADP A T221 D222 I226 Y227 D230 R232 K257 V258 T219 D220 I224 Y225 D228 R230 K255 V256
Gene Ontology
Molecular Function
GO:0004072 aspartate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009085 lysine biosynthetic process
GO:0009089 lysine biosynthetic process via diaminopimelate
GO:0009090 homoserine biosynthetic process
GO:0016310 phosphorylation
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:2j0w, PDBe:2j0w, PDBj:2j0w
PDBsum2j0w
PubMed16905770
UniProtP08660|AK3_ECOLI Lysine-sensitive aspartokinase 3 (Gene Name=lysC)

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