Structure of PDB 1j20 Chain D

Receptor sequence
>1j20D (length=386) Species: 274 (Thermus thermophilus) [Search protein sequence]
MKIVLAYSGGLDTSIILKWLKETYRAEVIAFTADIGQGEEVEEAREKALR
TGASKAIALDLKEEFVRDFVFPMMRAGAVYEGYYLLGTSIARPLIAKHLV
RIAEEEGAEAIAHGATGKGNDQVRFELTAYALKPDIKVIAPWREWSFQGR
KEMIAYAEAHGIPVPPYSMDANLLHISYEGGVLEDPWAEPPKGMFRMTQD
PEEAPDAPEYVEVEFFEGDPVAVNGERLSPAALLQRLNEIGGRHGVGRVD
IVENRFVGMKSRGVYETPGGTILYHARRAVESLTLDREVLHQRDMLSPKY
AELVYYGFWYAPEREALQAYFDHVARSVTGVARLKLYKGNVYVVGRKAPK
SLYRQDLVSFGYDQKDAEGFIKIQALRLRVRALVER
3D structure
PDB1j20 Structures of argininosuccinate synthetase in enzyme-ATP-substrates and enzyme-AMP-product forms
ChainD
Resolution2.0 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 AMP D A6 Y7 T13 A33 Q37 R92 G114 F125 A6 Y7 T13 A33 Q37 R92 G114 F125
BS02 AS1 D Y84 T88 A115 T116 G119 N120 D121 R124 S182 E184 E258 Y270 Y310 Y84 T88 A115 T116 G119 N120 D121 R124 S177 E179 E253 Y265 Y305
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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Biological Process
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Cellular Component
External links
PDB RCSB:1j20, PDBe:1j20, PDBj:1j20
PDBsum1j20
PubMed12684518
UniProtP59846|ASSY_THET8 Argininosuccinate synthase (Gene Name=argG)

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