Structure of PDB 1j21 Chain A

Receptor sequence

>1j21A (length=380) Species: 274 (Thermus thermophilus)

MKIVLAYSGGLDTSIILKWLKETYRAEVIAFTADIGQGEEVEEAREKALR
TGASKAIALDLKEEFVRDFVFPMMRAGAVYEGYYLLGTSIARPLIAKHLV
RIAEEEGAEAIAHGATGKGNDQVRFELTAYALKPDIKVIAPWREWSFQGR
KEMIAYAEAHGIPVPPYSMDANLLHISYEGGVLEDPWAEPPKGMFRMTQD
PEEAPDAPEYVEVEFFEGDPVAVNGERLSPAALLQRLNEIGGRHGVGRVD
IVENRFVGMKSRGVYETPGGTILYHARRAVESLTLDREVLHQRDMLSPKY
AELVYYGFWYAPEREALQAYFDHVARSVTGVARLKLYKGNVYVVGRKAPK
SLYRGYDQKDAEGFIKIQALRLRVRALVER

3D structure

• PDB: 1j21 Structures of argininosuccinate synthetase in enzyme-ATP-substrates and enzyme-AMP-product forms
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D12 R92 D121 S173
• Catalytic site (residue number reindexed from 1): D12 R92 D121 S168
• Enzyme Commision number: 6.3.4.5: argininosuccinate synthase.

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	ATP	A	A6 S8 G10 D12 T13 A33 I95 H113 G114 F125	A6 S8 G10 D12 T13 A33 I95 H113 G114 F125
BS02	CIR	A	Y84 T88 R124 S173 M174 S182 E184 E258 Y270	Y84 T88 R124 S168 M169 S177 E179 E253 Y265

Gene Ontology

Molecular Function

• GO:0004055 argininosuccinate synthase activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity

Biological Process

• GO:0000050 urea cycle
• GO:0000053 argininosuccinate metabolic process
• GO:0006526 L-arginine biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1j21, PDBe:1j21, PDBj:1j21
• PDBsum: 1j21
• PubMed: 12684518
• UniProt: P59846|ASSY_THET8 Argininosuccinate synthase (Gene Name=argG)