Structure of PDB 2y4s Chain A

Receptor sequence
>2y4sA (length=863) Species: 4513 (Hordeum vulgare) [Search protein sequence]
FMPDARAYWVTSDLIAWNVGSVCLYASRAAAMSLQGYDSKVELQPESAGL
PETVTQKFPFISSYRAFRVPSSVDVASLVKCQLVVASDVTGLQLPGVLDD
MFAYTGPLGAVFSEDSVSLHLWAPTAQGVSVCFFDGPAGPALETVQLKES
NGVWSVTGPREWENRYYLYEVDVYHPTKAQVLKCLAGDPYARSLSANGAR
TWLVDINNETLKPASWDELADEKPKLDSFSDITIYELHIRDFSAHDGTVD
SDSRGGFRAFAYQASAGMEHLRKLSDAGLTHVHLLPSFHFAGVDDIKSNW
KFVDECELATFPPGSDMQQAAVVAIQEEDPYNWGYNPVLWGVPKGSYASD
PDGPSRIIEYRQMVQALNRIGLRVVMDVVYNHLDSSGPCGISSVLDKIVP
GYYVRRDTNGQIENSAAMNNTASEHFMVDRLIVDDLLNWAVNYKVDGFRF
DLMGHIMKRTMMRAKSALQSLTTDAHGVDGSKIYLYGEGWDFAEVARNQR
GINGSQLNMSGTGIGSFNDRIRDAINGGNPFGNPLQQGFNTGLFLEPNGF
YQGNEADTRRSLATYADQIQIGLAGNLRDYVLISHTGEAKKGSEIHTFDG
LPVGYTASPIETINYVSAHDNETLFDVISVKTPMILSVDERCRINHLASS
MMALSQGIPFFHAGDEILRSKSIDRDSYNSGDWFNKLDFTYETNNWGVGL
PPSEKNEDNWPLMKPRLENPSFKPAKGHILAALDSFVDILKIRYSSPLFR
LSTANDIKQRVRFHNTGPSLVPGVIVMGIEDARGESPEMAQLDTNFSYVV
TVFNVCPHEVSMDIPALASMGFELHPVQVNSSDTLVRKSAYEAATGRFTV
PGRTVSVFVEPRC
3D structure
PDB2y4s Crystal Structure of an Essential Enzyme in Seed Starch Degradation: Barley Limit Dextrinase in Complex with Cyclodextrins.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N219 H311 F312 K366 D473 E510 D642
Catalytic site (residue number reindexed from 1) N197 H289 F290 K344 D451 E488 D620
Enzyme Commision number 3.2.1.41: pullulanase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0051060 pullulanase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2y4s, PDBe:2y4s, PDBj:2y4s
PDBsum2y4s
PubMed20863834
UniProtQ9S7S8

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