Structure of PDB 1lon Chain A

Receptor sequence
>1lonA (length=431) Species: 10090 (Mus musculus) [Search protein sequence]
AATGSRVTVVLGAQWGDEGKGKVVDLLATDADIVSRCQGGNNAGHTVVVD
GKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKGLKDWEK
RLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAA
RTGLRICDLLSDFDEFSARFKNLAHQHQSMFPTLEIDVEGQLKRLKGFAE
RIRPMVRDGVYFMYEALHGPPKKVLVEGANAALLDIDFGTYPFVTSSNCT
VGGVCTGLGIPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGDLLQNRG
HEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDVLSEIKVG
ISYKLNGKRIPYFPANQEILQKVEVEYETLPGWKADTTGARKWEDLPPQA
QSYVRFVENHMGVAVKWVGVGKSRESMIQLF
3D structure
PDB1lon IMP, GTP, and 6-phosphoryl-IMP complexes of recombinant mouse muscle adenylosuccinate synthetase.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D43 K46 G70 H71 N256
Catalytic site (residue number reindexed from 1) D17 K20 G44 H45 N230
Enzyme Commision number 6.3.4.4: adenylosuccinate synthase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0004019 adenylosuccinate synthase activity
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006163 purine nucleotide metabolic process
GO:0006164 purine nucleotide biosynthetic process
GO:0006167 AMP biosynthetic process
GO:0044208 'de novo' AMP biosynthetic process
GO:0044209 AMP salvage
Cellular Component
GO:0005737 cytoplasm
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1lon, PDBe:1lon, PDBj:1lon
PDBsum1lon
PubMed12004071
UniProtP28650|PURA1_MOUSE Adenylosuccinate synthetase isozyme 1 (Gene Name=Adss1)

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