Structure of PDB 1dj2 Chain A

Receptor sequence
>1dj2A (length=429) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
IGSLSQVSGVLGCQWGDEGKGKLVDILAQHFDIVARCQGGANAGHTIYNS
EGKKFALHLVPSGILNEDTTCVIGNGVVVHLPGLFKEIDGLESNGVSCKG
RILVSDRAHLLFDFHQEVDGLRESELAKSFIGTTKRGIGPAYSSKVIRNG
IRVGDLRHMDTLPQKLDLLLSDAAARFQGFKYTPEMLREEVEAYKRYADR
LEPYITDTVHFINDSISQKKKVLVEGGQATMLDIDFGTYPFVTSSSPSAG
GICTGLGIAPSVVGDLIGVVKAYTTRVGSGPFPTENLGTGGDLLRLAGQE
FGTTTGRPRRCGWLDIVALKFSCQINGFASLNLTKLDVLSDLNEIQLGVA
YKRSDGTPVKSFPGDLRLLEELHVEYEVLPGWKSDISSVRNYSDLPKAAQ
QYVERIEELVGVPIHYIGIGPGRDALIYK
3D structure
PDB1dj2 Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana.
ChainA
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D31 K34 G58 H59 Q242
Catalytic site (residue number reindexed from 1) D17 K20 G44 H45 Q228
Enzyme Commision number 6.3.4.4: adenylosuccinate 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 GDP A G30 D31 G33 K34 G58 H59 T60 K349 D351 G432 G434 P435 G16 D17 G19 K20 G44 H45 T46 K335 D337 G418 G420 P421
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0004019 adenylosuccinate synthase activity
GO:0005525 GTP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006167 AMP biosynthetic process
GO:0044208 'de novo' AMP biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0009507 chloroplast
GO:0009536 plastid
GO:0009570 chloroplast stroma
GO:0048046 apoplast

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Molecular Function
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Cellular Component
External links
PDB RCSB:1dj2, PDBe:1dj2, PDBj:1dj2
PDBsum1dj2
PubMed10669609
UniProtQ96529|PURA_ARATH Adenylosuccinate synthetase, chloroplastic (Gene Name=PURA)

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