Structure of PDB 2isw Chain A Binding Site BS01

Receptor Information
>2isw Chain A (length=307) Species: 5741 (Giardia intestinalis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PLCTLRQMLGEARKHKYGVGAFNVNNMEQIQGIMKAVVQLKSPVILQCSR
GALKYSDMIYLKKLCEAALEKHPDIPICIHLDHGDTLESVKMAIDLGFSS
VMIDASHHPFDENVRITKEVVAYAHARSVSVEAELGTLVQLTEPQDAKKF
VELTGVDALAVAIGTSHGAYKFKSRLAIDRVKTISDLTGIPLVMHGSSSV
PKDVKDMINKYGGKMPDAVGVPIESIVHAIGEGVCKINVDSDSRMAMTGA
IRKVFVEHPEKFDPRDYLGPGRDAITEMLIPKIKAFGSAGHAGDYKVVSL
EEAKAWY
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain2isw Chain A Residue 326 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2isw Characterization, kinetics, and crystal structures of fructose-1,6-bisphosphate aldolase from the human parasite, Giardia lamblia.
Resolution1.75 Å
Binding residue
(original residue number in PDB)		H84 H178 H210
Binding residue
(residue number reindexed from 1)		H83 H167 H195
Annotation score1
Enzymatic activity
Enzyme Commision number 4.1.2.13: fructose-bisphosphate aldolase.
Gene Ontology
Molecular Function
GO:0004332 fructose-bisphosphate aldolase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0016832 aldehyde-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006096 glycolytic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2isw, PDBe:2isw, PDBj:2isw
PDBsum2isw
PubMed17166851
UniProtA8B2U2|ALF_GIAIC Fructose-bisphosphate aldolase (Gene Name=fba)

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