Structure of PDB 2ac1 Chain A

Receptor sequence

>2ac1A (length=537) Species: 3702 (Arabidopsis thaliana)

NQPYRTGFHFQPPKNWMNDPNGPMIYKGIYHLFYQWNPKGAVWGNIVWAH
STSTDLINWDPHPPAIFPSAPFDINGCWSGSATILPNGKPVILYTGIDPK
NQQVQNIAEPKNLSDPYLREWKKSPLNPLMAPDAVNGINASSFRDPTTAW
LGQDKKWRVIIGSKIHRRGLAITYTSKDFLKWEKSPEPLHYDDGSGMWEC
PDFFPVTRFGSNGVETSSFGEPNEILKHVLKISLDDTKHDYYTIGTYDRV
KDKFVPDNGFKMDGTAPRYDYGKYYASKTFFDSAKNRRILWGWTNESSSV
EDDVEKGWSGIQTIPRKIWLDRSGKQLIQWPVREVERLRTKQVKNLRNKV
LKSGSRLEVYGVTAAQADVEVLFKVRDLEKADVIEPSWTDPQLICSKMNV
SVKSGLGPFGLMVLASKNLEEYTSVYFRIFKARQNSNKYVVLMCSDQSRS
SLKEDNDKTTYGAFVDINPHQPLSLRALIDHSVVESFGGKGRACITSRVY
PKLAIGKSSHLFAFNYGYQSVDVLNLNAWSMNSAQIS

3D structure

• PDB: 2ac1 X-ray diffraction structure of a cell-wall invertase from Arabidopsis thaliana.
• Chain: A
• Resolution: 2.15 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D23 E203
• Catalytic site (residue number reindexed from 1): D19 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	MAN	A	Q396 S400	Q392 S396

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:2ac1, PDBe:2ac1, PDBj:2ac1
• PDBsum: 2ac1
• PubMed: 17139091
• UniProt: Q43866|INV1_ARATH Beta-fructofuranosidase, insoluble isoenzyme CWINV1 (Gene Name=CWINV1)