Structure of PDB 3ugg Chain A

Receptor sequence
>3uggA (length=524) Species: 74825 (Pachysandra terminalis) [Search protein sequence]
PYPWSNAQLSWQRTAFHFQPERSWMSDPDGPIFYKGWYHFFYQYNPDNPV
WGNNTWGHTVSRDLIHWLYLPLALAADQWYDMQGVFSGSATCLPDGRIMM
LYTGVTKEMVEMLSLAYPADLSDPLLVEWVKYPGNPILSAPPGVSPTEFR
DASTGWYVSNGTWRIAIGAKYNTTGIAMVYETKDFKSFKLLEELLHAVPD
TGLWECVDLYPVSTTGEKGLETSVNGPKVKHVLKASIDEQQRDYYAIGTY
DLGTNKWTPDNPEEDVGIGLRYDWGKYYASKTFYDPKKQRRVVWAWTKEL
DSEVADREKGWANVQTIPRTVLLDQKTGTNVLLWPVEEVESLRLSSKEFS
KVKAGAGSVVPLDVGTATQLDIIAEFEIDKGYNCTTSGGAAERGVLGPFG
LLVSATENLSEQTPVYFYIAKNFKTFFCLDESRSSKASDVSKQVKGFTVP
VLDGEKFTMRLLVDHSIVESFAQGGRSCITSRVYPTEAIYGAAKLFLFNN
ATGASITASLKIWEMNSAFIQPFH
3D structure
PDB3ugg Crystal structure of 6-SST/6-SFT from Pachysandra terminalis, a plant fructan biosynthesizing enzyme in complex with its acceptor substrate 6-kestose.
ChainA
Resolution2.9 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) D33 E211
Catalytic site (residue number reindexed from 1) D27 E205
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 E211 D244 E205 D238
BS02 FRU A D33 Q49 W57 S93 D157 E211 Y284 D27 Q43 W51 S87 D151 E205 Y278
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3ugg, PDBe:3ugg, PDBj:3ugg
PDBsum3ugg
PubMed22098191
UniProtE3PQS3

[Back to BioLiP]