Structure of PDB 1q1g Chain A Binding Site BS01

Receptor Information
>1q1g Chain A (length=243) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NLLRHLKISKEQITPVVLVVGDPGRVDKIKVVCDSYVDLAYNREYKSVEC
HYKGQKFLCVSHGVGSAGCAVCFEELCQNGAKVIIRAGSCGSLQPDLIKR
GDICICNAAVREDRVSHLLIHGDFPAVGDFDVYDTLNKCAQELNVPVFNG
ISVSSDMYYPNKIIPSRLEDYSKANAAVVEMELATLMVIGTLRKVKTGGI
LIVDGCPFKWDEGDFDNNLVPHQLENMIKIALGACAKLATKYA
Ligand information
Ligand IDMTI
InChIInChI=1S/C12H16N4O3S/c1-20-3-6-10(17)11(18)8(16-6)5-2-13-9-7(5)14-4-15-12(9)19/h2,4,6,8,10-11,13,16-18H,3H2,1H3,(H,14,15,19)/p+1/t6-,8+,10-,11+/m1/s1
InChIKeyCEGIKIXYDFDYDN-RXDXJJGDSA-O
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CSCC1C(C(C([NH2+]1)c2c[nH]c3c2N=CNC3=O)O)O
ACDLabs 10.04O=C1c2c(N=CN1)c(cn2)C3[NH2+]C(CSC)C(O)C3O
OpenEye OEToolkits 1.5.0CSC[C@@H]1[C@H]([C@H]([C@@H]([NH2+]1)c2c[nH]c3c2N=CNC3=O)O)O
CACTVS 3.341CSC[C@H]1[NH2+][C@H]([C@H](O)[C@@H]1O)c2c[nH]c3C(=O)NC=Nc23
CACTVS 3.341CSC[CH]1[NH2+][CH]([CH](O)[CH]1O)c2c[nH]c3C(=O)NC=Nc23
FormulaC12 H17 N4 O3 S
Name3,4-DIHYDROXY-2-[(METHYLSULFANYL)METHYL]-5-(4-OXO-4,5-DIHYDRO-3H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)PYRROLIDINIUM;
(1S)-1-(0-DEAZAHYPOXANTHIN-9-YL)-1,4-DIDEOXY-1,4-IMINO-5-METHYLTHIO-D-RIBITOL;
MT-IMMUCILLIN-H;
MT-IMMH
ChEMBL
DrugBankDB03881
ZINC
PDB chain1q1g Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1q1g Plasmodium falciparum Purine Nucleoside Phosphorylase: CRYSTAL STRUCTURES, IMMUCILLIN INHIBITORS, AND DUAL CATALYTIC FUNCTION.
Resolution2.02 Å
Binding residue
(original residue number in PDB)		V66 S91 C92 G93 Y160 E182 M183 E184 D206
Binding residue
(residue number reindexed from 1)		V64 S89 C90 G91 Y158 E180 M181 E182 D204
Annotation score1
Binding affinityMOAD: Kd=2.7nM
PDBbind-CN: -logKd/Ki=8.57,Kd=2.7nM
Enzymatic activity
Catalytic site (original residue number in PDB) H7 G23 R27 R45 E77 R88 S91 D206 G207 P209 V222
Catalytic site (residue number reindexed from 1) H5 G21 R25 R43 E75 R86 S89 D204 G205 P207 V220
Enzyme Commision number 2.4.2.1: purine-nucleoside phosphorylase.
2.4.2.44: S-methyl-5'-thioinosine phosphorylase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside phosphorylase activity
GO:0004850 uridine phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0017061 S-methyl-5-thioadenosine phosphorylase activity
GO:0047975 guanosine phosphorylase activity
Biological Process
GO:0006148 inosine catabolic process
GO:0006166 purine ribonucleoside salvage
GO:0006195 purine nucleotide catabolic process
GO:0006218 uridine catabolic process
GO:0009116 nucleoside 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:1q1g, PDBe:1q1g, PDBj:1q1g
PDBsum1q1g
PubMed14982926
UniProtQ8I3X4|PNPH_PLAF7 Purine nucleoside phosphorylase (Gene Name=PNP)

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