Structure of PDB 2oxb Chain A

Receptor sequence
>2oxbA (length=537) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
NQPYRTGFHFQPPKNWMNDPNGPMIYKGIYHLFYQWNPKGAVWGNIVWAH
STSTDLINWDPHPPAIFPSAPFDINGCWSGSATILPNGKPVILYTGIDPK
NQQVQNIAEPKNLSDPYLREWKKSPLNPLMAPDAVNGINASSFRDPTTAW
LGQDKKWRVIIGSKIHRRGLAITYTSKDFLKWEKSPEPLHYDDGSGMWQC
PDFFPVTRFGSNGVETSSFGEPNEILKHVLKISLDDTKHDYYTIGTYDRV
KDKFVPDNGFKMDGTAPRYDYGKYYASKTFFDSAKNRRILWGWTNESSSV
EDDVEKGWSGIQTIPRKIWLDRSGKQLIQWPVREVERLRTKQVKNLRNKV
LKSGSRLEVYGVTAAQADVEVLFKVRDLEKADVIEPSWTDPQLICSKMNV
SVKSGLGPFGLMVLASKNLEEYTSVYFRIFKARQNSNKYVVLMCSDQSRS
SLKEDNDKTTYGAFVDINPHQPLSLRALIDHSVVESFGGKGRACITSRVY
PKLAIGKSSHLFAFNYGYQSVDVLNLNAWSMNSAQIS
3D structure
PDB2oxb An alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: An X-ray crystallography and docking study.
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D23 Q203
Catalytic site (residue number reindexed from 1) D19 Q199
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 FRU A D23 Q39 W47 W82 S83 D149 Q203 Y279 D19 Q35 W43 W78 S79 D145 Q199 Y275
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2oxb, PDBe:2oxb, PDBj:2oxb
PDBsum2oxb
PubMed17963237
UniProtQ43866|INV1_ARATH Beta-fructofuranosidase, insoluble isoenzyme CWINV1 (Gene Name=CWINV1)

[Back to BioLiP]