Structure of PDB 2qqw Chain A Binding Site BS03

Receptor Information
>2qqw Chain A (length=534) Species: 3702 (Arabidopsis thaliana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NQPYRTGFHFQPPKNWMNAPNGPMIYKGIYHLFYQWNPKGAVWGNIVWAH
STSTDLINWDPHPPAIFPSAPFDINGCWSGSATILPNGKPVILYTGIDPK
NQQVQNIAEPKNLSDPYLREWKKSPLNPLMAPDAVNGINASSFRDPTTAW
LGQDKKWRVIIGSKIHRRGLAITYTSKDFLKWEKSPEPLHYDDGSGMWEC
PDFFPVTRFGSNGVETSSFGEPNEILKHVLKISLDDTKHDYYTIGTYDRV
KDKFVPDNGFGTAPRYDYGKYYASKTFFDSAKNRRILWGWTNESSSVEDD
VEKGWSGIQTIPRKIWLDRSGKQLIQWPVREVERLRTKQVKNLRNKVLKS
GSRLEVYGVTAAQADVEVLFKVRDLEKADVIEPSWTDPQLICSKMNVSVK
SGLGPFGLMVLASKNLEEYTSVYFRIFKARQNSNKYVVLMCSDQSRSSLK
EDNDKTTYGAFVDINPHQPLSLRALIDHSVVESFGGKGRACITSRVYPKL
AIGKSSHLFAFNYGYQSVDVLNLNAWSMNSAQIS
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 chain2qqw Chain A Residue 1102 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2qqw Crystal structures of Arabidopsis thaliana cell-wall invertase mutants in complex with sucrose.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		H194 D196
Binding residue
(residue number reindexed from 1)		H190 D192
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) A23 E203
Catalytic site (residue number reindexed from 1) A19 E199
Enzyme Commision number 3.2.1.26: beta-fructofuranosidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004564 beta-fructofuranosidase activity
GO:0005515 protein binding
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009611 response to wounding
GO:0050832 defense response to fungus
Cellular Component
GO:0005886 plasma membrane
GO:0048046 apoplast

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2qqw, PDBe:2qqw, PDBj:2qqw
PDBsum2qqw
PubMed18258263
UniProtQ43866|INV1_ARATH Beta-fructofuranosidase, insoluble isoenzyme CWINV1 (Gene Name=CWINV1)

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