Structure of PDB 4j3u Chain A

Receptor sequence
>4j3uA (length=870) Species: 4513 (Hordeum vulgare) [Search protein sequence]
MPDARAYWVTSDLIAWNVGELEQSVCLYASRAAAMSLSGIQGYDSKVELQ
PESAGLPETVTQKFPFISSYRAFRVPSSVDVASLVKCQLVVASFDVTGLQ
LPGVLDDMFAYTGPLGAVFSEDSVSLHLWAPTAQGVSVCFFDGPAGPALE
TVQLKESNGVWSVTGPREWENRYYLYEVDVYHPTKAQVLKCLAGDPYARS
LSANGARTWLVDINNETLKPASWDELADEKPKLDSFSDITIYELHIRDFS
AHDGTVDSDSRGGFRAFAYQASAGMEHLRKLSDAGLTHVHLLPSFHFAGV
DDIKSNWKFVDECELATFPPGSDMQQAAVVAIQEEDPYNWGYNPVLWGVP
KGSYASDPDGPSRIIEYRQMVQALNRIGLRVVMDVVYNHLDSSGPCGISS
VLDKIVPGYYVRRDTNGQIENSAAMNNTASEHFMVDRLIVDDLLNWAVNY
KVDGFRFDLMGHIMKRTMMRAKSALQSLTTDAHGVDGSKIYLYGEGWDFA
EVARNQRGINGSQLNMSGTGIGSFNDRIRDAINGGNPFGNPLQQGFNTGL
FLEPNGFYQGNEADTRRSLATYADQIQIGLAGNLRDYVLISHTGEAKKGS
EIHTFDGLPVGYTASPIETINYVSAHDNETLFDVISVKTPMILSVDERCR
INHLASSMMALSQGIPFFHAGDEILRSKSIDRDSYNSGDWFNKLDFTYET
NNWGVGLPPSEKNEDNWPLMKPRLENPSFKPAKGHILAALDSFVDILKIR
YSSPLFRLSTANDIKQRVRFHNTGPSLVPGVIVMGIEDARGESPEMAQLD
TNFSYVVTVFNVCPHEVSMDIPALASMGFELHPVQVNSSDTLVRKSAYEA
ATGRFTVPGRTVSVFVEPRC
3D structure
PDB4j3u Oligosaccharide and substrate binding in the starch debranching enzyme barley limit dextrinase
ChainA
Resolution1.7 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) N204 H296 F297 K351 D458 E495 D627
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 SGD A F514 D541 R544 F499 D526 R529 PDBbind-CN: -logKd/Ki=6.34,Ki=0.46uM
BS02 GLC A W512 N643 W497 N628 PDBbind-CN: -logKd/Ki=6.34,Ki=0.46uM
BS03 GLC A N551 F553 N536 F538 PDBbind-CN: -logKd/Ki=6.34,Ki=0.46uM
BS04 GLC A F514 F553 F499 F538 PDBbind-CN: -logKd/Ki=6.34,Ki=0.46uM
BS05 CA A S297 L301 G393 S282 L286 G378
BS06 CA A Q348 D351 Y353 N701 Q333 D336 Y338 N686
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0046872 metal ion binding
GO:0051060 pullulanase activity
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4j3u, PDBe:4j3u, PDBj:4j3u
PDBsum4j3u
PubMed25562209
UniProtQ9FYY0

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