Structure of PDB 2qqw Chain A

Receptor sequence

>2qqwA (length=534) Species: 3702 (Arabidopsis thaliana)

NQPYRTGFHFQPPKNWMNAPNGPMIYKGIYHLFYQWNPKGAVWGNIVWAH
STSTDLINWDPHPPAIFPSAPFDINGCWSGSATILPNGKPVILYTGIDPK
NQQVQNIAEPKNLSDPYLREWKKSPLNPLMAPDAVNGINASSFRDPTTAW
LGQDKKWRVIIGSKIHRRGLAITYTSKDFLKWEKSPEPLHYDDGSGMWEC
PDFFPVTRFGSNGVETSSFGEPNEILKHVLKISLDDTKHDYYTIGTYDRV
KDKFVPDNGFGTAPRYDYGKYYASKTFFDSAKNRRILWGWTNESSSVEDD
VEKGWSGIQTIPRKIWLDRSGKQLIQWPVREVERLRTKQVKNLRNKVLKS
GSRLEVYGVTAAQADVEVLFKVRDLEKADVIEPSWTDPQLICSKMNVSVK
SGLGPFGLMVLASKNLEEYTSVYFRIFKARQNSNKYVVLMCSDQSRSSLK
EDNDKTTYGAFVDINPHQPLSLRALIDHSVVESFGGKGRACITSRVYPKL
AIGKSSHLFAFNYGYQSVDVLNLNAWSMNSAQIS

3D structure

• PDB: 2qqw Crystal structures of Arabidopsis thaliana cell-wall invertase mutants in complex with sucrose.
• Chain: A
• Resolution: 2.8 Å

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.

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	GLC	A	W82 E203 D239	W78 E199 D235
BS02	FRU	A	N22 Q39 W47 W82 S83 R148 D149 E203	N18 Q35 W43 W78 S79 R144 D145 E199
BS03	ZN	A	H194 D196	H190 D192

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

External links

• PDB: RCSB:2qqw, PDBe:2qqw, PDBj:2qqw
• PDBsum: 2qqw
• PubMed: 18258263
• UniProt: Q43866|INV1_ARATH Beta-fructofuranosidase, insoluble isoenzyme CWINV1 (Gene Name=CWINV1)