Structure of PDB 2qga Chain B

Receptor sequence
>2qgaB (length=454) Species: 5855 (Plasmodium vivax) [Search protein sequence]
EHLKNISPIDGRYKKACGELSAFFSEHALIKHRIIVEVRWLLFLNEEELF
FEKVTDHSVEVLNQIATNITDSDIARVKAIEEETNHDVKAVEYFVKEKLK
NSKREDLLKIKEYVHYLCTSEDINNVAYATCLKACLNDVVIPCLEKIMLK
LKDLAVEYSHVPLLSRTHGQPASSTTFGKEMANFYARIHHHVGVIRRVKV
CAKFNGAVGNFNAHKVASKDTDWVNTIGLFLKKHFNLTYSIYCTQIQDHD
YICELCDGLARANGTLIDLCVDIWLYISNNLLKLKSSTMPHKVNPIDFEN
AEGNLHIANAFFKLFSSKLPTSRLQRDLSDSTVLRNIGSSLAYCLIAYKS
VLKGLNKIDIDRRNLEEELNQNWSTLAEPIQIVMKRHNYVDAYEELKQFT
RGKVIDQKIMQEFIKTKCAFLPQDVVDQLLELTPATYTGYADYLAKNVER
LSGE
3D structure
PDB2qga Plasmodium vivax adenylosuccinate lyase Pv003765 with AMP bound
ChainB
Resolution2.01 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H86 T167 H168 S294 K299 E306
Catalytic site (residue number reindexed from 1) H86 T167 H168 S287 K292 E299
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 B H86 D87 Q245 R333 L335 S338 T339 R342 H86 D87 Q245 R326 L328 S331 T332 R335
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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