Structure of PDB 2qga Chain C

Receptor sequence
>2qgaC (length=455) Species: 5855 (Plasmodium vivax) [Search protein sequence]
EHLKNISPIDGRYKKACGELSAFFSEHALIKHRIIVEVRWLLFLNEEELF
FEKVTDHSVEVLNQIATNITDSDIARVKAIEEETNHDVKAVEYFVKEKLK
NSKREDLLKIKEYVHYLCTSEDINNVAYATCLKACLNDVVIPCLEKIMLK
LKDLAVEYSHVPLLSRTHGQPASSTTFGKEMANFYARIHHHVGVIRRVKV
CAKFNGAVGNFNAHKVASKDTDWVNTIGLFLKKHFNLTYSIYCTQIQDHD
YICELCDGLARANGTLIDLCVDIWLYISNNLLKLKVGSSTMPHKVNPIDF
ENAEGNLHIANAFFKLFSSKLPTSRLQRDLSDSTVLRNIGSSLAYCLIAY
KSVLKGLNKIDIDRRNLEEELNQNWSTLAEPIQIVMKRHNYVDAYEELKQ
FTRGKVIDQKIMQEFIKTKCAFLPQDVVDQLLELTPATYTGYADYLAKNV
ERLSG
3D structure
PDB2qga Plasmodium vivax adenylosuccinate lyase Pv003765 with AMP bound
ChainC
Resolution2.01 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.3.2.2: adenylosuccinate lyase.
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 C N85 H86 D87 Q245 R333 S338 T339 R342 N85 H86 D87 Q245 R328 S333 T334 R337
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004018 N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
GO:0070626 (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006188 IMP biosynthetic process
GO:0006189 'de novo' IMP biosynthetic process
GO:0009152 purine ribonucleotide biosynthetic process
GO:0044208 'de novo' AMP biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2qga, PDBe:2qga, PDBj:2qga
PDBsum2qga
PubMed
UniProtA5KBL5

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