Structure of PDB 1j21 Chain C

Receptor sequence
>1j21C (length=380) Species: 274 (Thermus thermophilus) [Search protein sequence]
MKIVLAYSGGLDTSIILKWLKETYRAEVIAFTADIGQGEEVEEAREKALR
TGASKAIALDLKEEFVRDFVFPMMRAGAVYEGYYLLGTSIARPLIAKHLV
RIAEEEGAEAIAHGATGKGNDQVRFELTAYALKPDIKVIAPWREWSFQGR
KEMIAYAEAHGIPVPPYSMDANLLHISYEGGVLEDPWAEPPKGMFRMTQD
PEEAPDAPEYVEVEFFEGDPVAVNGERLSPAALLQRLNEIGGRHGVGRVD
IVENRFVGMKSRGVYETPGGTILYHARRAVESLTLDREVLHQRDMLSPKY
AELVYYGFWYAPEREALQAYFDHVARSVTGVARLKLYKGNVYVVGRKAPK
SLYRGYDQKDAEGFIKIQALRLRVRALVER
3D structure
PDB1j21 Structures of argininosuccinate synthetase in enzyme-ATP-substrates and enzyme-AMP-product forms
ChainC
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 C A6 S8 G10 L11 D12 T13 A33 I95 H113 G114 F125 A6 S8 G10 L11 D12 T13 A33 I95 H113 G114 F125
BS02 CIR C Y84 T88 R124 S173 M174 D175 S182 E184 E258 Y270 Y84 T88 R124 S168 M169 D170 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1j21, PDBe:1j21, PDBj:1j21
PDBsum1j21
PubMed12684518
UniProtP59846|ASSY_THET8 Argininosuccinate synthase (Gene Name=argG)

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