Structure of PDB 1kh3 Chain D

Receptor sequence
>1kh3D (length=386) Species: 274 (Thermus thermophilus) [Search protein sequence]
MKIVLAYSGGLDTSIILKWLKETYRAEVIAFTADIGQGEEVEEAREKALR
TGASKAIALDLKEEFVRDFVFPMMRAGAVYEGYYLLGTSIARPLIAKHLV
RIAEEEGAEAIAHGATGKGNDQVRFELTAYALKPDIKVIAPWREWSFQGR
KEMIAYAEAHGIPVPPYSMDANLLHISYEGGVLEDPWAEPPKGMFRMTQD
PEEAPDAPEYVEVEFFEGDPVAVNGERLSPAALLQRLNEIGGRHGVGRVD
IVENRFVGMKSRGVYETPGGTILYHARRAVESLTLDREVLHQRDMLSPKY
AELVYYGFWYAPEREALQAYFDHVARSVTGVARLKLYKGNVYVVGRKAPK
SLYRQDLVSFGYDQKDAEGFIKIQALRLRVRALVER
3D structure
PDB1kh3 Structures of Argininosuccinate Synthetase in Enzyme-ATP Substrates and Enzyme-AMP Product Forms: STEREOCHEMISTRY OF THE CATALYTIC REACTION
ChainD
Resolution2.15 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 ARG D Y84 T88 R124 S173 M174 D175 S182 E184 E258 Y270 Y310 Y84 T88 R124 S168 M169 D170 S177 E179 E253 Y265 Y305
BS02 ASP D A115 T116 G119 N120 D121 A115 T116 G119 N120 D121
BS03 ANP D A6 T32 A33 Q37 I95 H113 G114 F125 S173 M174 A6 T32 A33 Q37 I95 H113 G114 F125 S168 M169
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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Cellular Component
External links
PDB RCSB:1kh3, PDBe:1kh3, PDBj:1kh3
PDBsum1kh3
PubMed12684518
UniProtP59846|ASSY_THET8 Argininosuccinate synthase (Gene Name=argG)

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