Structure of PDB 4wio Chain A Binding Site BS01

Receptor Information
>4wio Chain A (length=525) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DKILVLNFGSQYFHLIVKRLNNIKIFSETKDYGVELKDIKDMNIKGVILS
GGPYSVTEAGSPHLKKEVFEYFLEKKIPIFGIAYGMQEIAVQMNGEVKKS
KTSEYGCTDVNILRNDNINNITYCRNFSSAMDLYSNYKLMNECLFENIKS
DITTVWMNHNDEVTKIPENFYLVSSSENCLICSIYNKEYNIYGVQYHPEV
YESLDGELMFYNFAYNICKCKKQFDPIRYHELELKNIEKYKHDHYVIAAM
SGGIDSTVAAAYTHKIFKERFFGIFIDNGLLRKNEAENVYTFLKSTFPDM
NITKIDASENFLSNLQGVTDPEQKRKIIGKLFIEEFEKAVNNIDIDINKT
FLLQGTLYPDIIESKCSKNLSDTIKTHHNLKFKLFEPFKYLFKDDVKTLS
RELNLPEEITNRHPFPGPGLAIRVIGEINKHKLNILREVDDIFINDLKQY
GLYNQISQAFAVLLSYDYVCVLRAVKTSSFMTANWYQIPYDILDKITTRI
LSEVKGVNRILYDVSSKPPATIEFE
Ligand information
Ligand IDGLN
InChIInChI=1S/C5H10N2O3/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H2,7,8)(H,9,10)/t3-/m0/s1
InChIKeyZDXPYRJPNDTMRX-VKHMYHEASA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(CC(=O)N)C(C(=O)O)N
OpenEye OEToolkits 1.5.0C(CC(=O)N)[C@@H](C(=O)O)N
ACDLabs 10.04O=C(N)CCC(N)C(=O)O
CACTVS 3.341N[CH](CCC(N)=O)C(O)=O
CACTVS 3.341N[C@@H](CCC(N)=O)C(O)=O
FormulaC5 H10 N2 O3
NameGLUTAMINE
ChEMBLCHEMBL930
DrugBankDB00130
ZINCZINC000001532526
PDB chain4wio Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4wio Active site coupling in Plasmodium falciparum GMP synthetase is triggered by domain rotation.
Resolution3.15 Å
Binding residue
(original residue number in PDB)		Q93 N169 H170 N171 D172 H208
Binding residue
(residue number reindexed from 1)		Q87 N158 H159 N160 D161 H197
Annotation score5
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).
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4wio, PDBe:4wio, PDBj:4wio
PDBsum4wio
PubMed26592566
UniProtQ8IJR9|GUAA_PLAF7 GMP synthase [glutamine-hydrolyzing] (Gene Name=GMPS)

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