Structure of PDB 2j0x Chain A

Receptor sequence

>2j0xA (length=447) Species: 562 (Escherichia coli)

EIVVSKFGGTSVADFDAMNRSADIVLSDANVRLVVLSASAGITNLLVALA
EGLEPGERFEKLDAIRNIQFAILERLRYPNVIREEIERLLENITVLAEAA
ALATSPALTDELVSHGELMSTLLFVEILRERDVQAQWFDVRKVMRTNDRF
GRAEPDIAALAELAALQLLPRLNEGLVITQGFIGSENKGRTTTLGRGGSD
YTAALLAEALHASRVDIWTDVPGIYTTDPRVVSAAKRIDEIAFAEAAEMA
TFGAKVLHPATLLPAVRSDIPVFVGSSKDPRAGGTLVCNKTENPPLFRAL
ALRRNQTLLTLHSLNMLHSRGFLAEVFGILARHNISVDLITTSEVSVALT
LDTTGSTSTGDTLLTQSLLMELSALCRVEVEEGLALVALIGNDLSKACGV
GKEVFGVLEPFNIRMICYGASSHNLCFLVPGEDAEQVVQKLHSNLFE

3D structure

• PDB: 2j0x Structures of R- and T-State Escherichia Coli Aspartokinase III: Mechanisms of the Allosteric Transition and Inhibition by Lysine.
• Chain: A
• Resolution: 2.8 Å

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	F184 G199 G200 S201 D202	F182 G197 G198 S199 D200
BS02	LYS	A	M318 S321 F324 L325 S345 E346	M316 S319 F322 L323 S343 E344
BS03	LYS	A	S338 V339 D340	S336 V337 D338

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

External links

• PDB: RCSB:2j0x, PDBe:2j0x, PDBj:2j0x
• PDBsum: 2j0x
• PubMed: 16905770
• UniProt: P08660|AK3_ECOLI Lysine-sensitive aspartokinase 3 (Gene Name=lysC)