Structure of PDB 4wio Chain A

Receptor sequence

>4wioA (length=525) Species: 36329 (Plasmodium falciparum 3D7)

DKILVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILS
GGPYSVTEAGSPHLKKEVFEYFLEKKIPIFGIAYGMQEIAVQMNGEVKKS
KTSEYGCTDVNILRNDNINNITYCRNFSSAMDLYSNYKLMNECLFENIKS
DITTVWMNHNDEVTKIPENFYLVSSSENCLICSIYNKEYNIYGVQYHPEV
YESLDGELMFYNFAYNICKCKKQFDPIRYHELELKNIEKYKHDHYVIAAM
SGGIDSTVAAAYTHKIFKERFFGIFIDNGLLRKNEAENVYTFLKSTFPDM
NITKIDASENFLSNLQGVTDPEQKRKIIGKLFIEEFEKAVNNIDIDINKT
FLLQGTLYPDIIESKCSKNLSDTIKTHHNLKFKLFEPFKYLFKDDVKTLS
RELNLPEEITNRHPFPGPGLAIRVIGEINKHKLNILREVDDIFINDLKQY
GLYNQISQAFAVLLSYDYVCVLRAVKTSSFMTANWYQIPYDILDKITTRI
LSEVKGVNRILYDVSSKPPATIEFE

3D structure

• PDB: 4wio Active site coupling in Plasmodium falciparum GMP synthetase is triggered by domain rotation.
• Chain: A
• Resolution: 3.15 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G58 A89 Y90 H208 E210 D266 K411
• Catalytic site (residue number reindexed from 1): G52 A83 Y84 H197 E199 D255 K393
• Enzyme Commision number: 6.3.5.2: GMP synthase (glutamine-hydrolyzing).

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	GLN	A	Q93 N169 H170 N171 D172 H208	Q87 N158 H159 N160 D161 H197

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003921 GMP synthase activity
• GO:0003922 GMP synthase (glutamine-hydrolyzing) activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006164 purine nucleotide biosynthetic process
• GO:0006177 GMP biosynthetic process
• GO:0006541 glutamine metabolic process
• GO:0046037 GMP metabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:4wio, PDBe:4wio, PDBj:4wio
• PDBsum: 4wio
• PubMed: 26592566
• UniProt: Q8IJR9|GUAA_PLAF7 GMP synthase [glutamine-hydrolyzing] (Gene Name=GMPS)