Structure of PDB 4aio Chain A

Receptor sequence
>4aioA (length=883) Species: 4513 (Hordeum vulgare) [Search protein sequence]
AFMPDARAYWVTSDLIAWNVGELEAQSVCLYASRAAAMSLSPSNGGIQGY
DSKVELQPESAGLPETVTQKFPFISSYRAFRVPSSVDVASLVKCQLVVAS
FGADGKHVDVTGLQLPGVLDDMFAYTGPLGAVFSEDSVSLHLWAPTAQGV
SVCFFDGPAGPALETVQLKESNGVWSVTGPREWENRYYLYEVDVYHPTKA
QVLKCLAGDPYARSLSANGARTWLVDINNETLKPASWDELADEKPKLDSF
SDITIYELHIRDFSAHDGTVDSDSRGGFRAFAYQASAGMEHLRKLSDAGL
THVHLLPSFHFAGVDDIKSNWKFVDECELATFPPGSDMQQAAVVAIQEED
PYNWGYNPVLWGVPKGSYASDPDGPSRIIEYRQMVQALNRIGLRVVMDVV
YNHLDSSGPCGISSVLDKIVPGYYVRRDTNGQIENSAAMNNTASEHFMVD
RLIVDDLLNWAVNYKVDGFRFDLMGHIMKRTMMRAKSALQSLTTDAHGVD
GSKIYLYGEGWDFAEVARNQRGINGSQLNMSGTGIGSFNDRIRDAINGGN
PFGNPLQQGFNTGLFLEPNGFYQGNEADTRRSLATYADQIQIGLAGNLRD
YVLISHTGEAKKGSEIHTFDGLPVGYTASPIETINYVSAHDNETLFDVIS
VKTPMILSVDERCRINHLASSMMALSQGIPFFHAGDEILRSKSIDRDSYN
SGDWFNKLDFTYETNNWGVGLPPSEKNEDNWPLMKPRLENPSFKPAKGHI
LAALDSFVDILKIRYSSPLFRLSTANDIKQRVRFHNTGPSLVPGVIVMGI
EDARGESPEMAQLDTNFSYVVTVFNVCPHEVSMDIPALASMGFELHPVQV
NSSDTLVRKSAYEAATGRFTVPGRTVSVFVEPR
3D structure
PDB4aio Structure of the Starch-Debranching Enzyme Barley Limit Dextrinase Reveals Homology of the N-Terminal Domain to Cbm21.
ChainA
Resolution1.9 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) N219 H311 F312 K366 D473 E510 D642
Catalytic site (residue number reindexed from 1) N218 H310 F311 K365 D472 E509 D641
Enzyme Commision number 3.2.1.41: pullulanase.
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 GOL A F324 D351 G703 D704 W705 F323 D350 G702 D703 W704
BS02 GOL A Y357 H404 A438 D473 Y356 H403 A437 D472
BS03 CA A Q348 D351 Y353 N701 Q347 D350 Y352 N700
BS04 CA A S297 L301 G393 S296 L300 G392
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0051060 pullulanase activity
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4aio, PDBe:4aio, PDBj:4aio
PDBsum4aio
PubMed22949184
UniProtO48541

[Back to BioLiP]