Structure of PDB 2x2j Chain A Binding Site BS01

Receptor Information
>2x2j Chain A (length=1025) Species: 2782 (Gracilariopsis lemaneiformis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TDNPDGIDYKTYDYVGVWGFSPLSNTNWFAAGSSTPGGITDWTATMNVNF
DRIDNPSITVQHPVQVQVTSYNNNSYRVRFNPDGPIRDVTRGPILKQQLD
WIRTQELSEGCDPGMTFTSEGFLTFETKDLSVIIYGNFKTRVTRKSDGKV
IMENDEVGTASSGNKCRGLMFVDRLYGNAIASVNKNFRNDAVKQEGFYGA
GEVNCKYQDTYILERTGIAMTNYNYDNLNYNQWDLRPPHHDGALNPDYYI
PMYYAAPWLIVNGCAGTSEQYSYGWFMDNVSQSYMNTGDTTWNSGQEDLA
YMGAQYGPFDQHFVYGAGGGMECVVTAFSLLQGKEFENQVLNKRSVMPPK
YVFGFFQGVFGTSSLLRAHMPAGENNISVEEIVEGYQNNNFPFEGLAVDV
DMQDNLRVFTTKGEFWTANRVGTGGDPNNRSVFEWAHDKGLVCQTNITCF
LRNDNEGQDYEVNQTLRERQLYTKNDSLTGTDFGMTDDGPSDAYIGHLDY
GGGVECDALFPDWGRPDVAEWWGNNYKKLFSIGLDFVWQDMTVPAMMPHK
IGDDINVKPDGNWPNADDPSNGQYNWKTYHPQVLVTDMRYENHGREPMVT
QRNIHAYTLCESTRKEGIVENADTLTKFRRSYIISRGGYIGNQHFGGMWV
GDNSTTSNYIQMMIANNINMNMSCLPLVGSDIGGFTSYDNENQRTPCTGD
LMVRYVQAGCLLPWFRNHYDRWIESKDHGKDYQELYMYPNEMDTLRKFVE
FRYRWQEVLYTAMYQNAAFGKPIIKAASMYNNDSNVRRAQNDHFLLGGHD
GYRILCAPVVWENSTERELYLPVLTQWYKFGPDFDTKPLEGAMNGGDRIY
NYPVPQSESPIFVREGAILPTRYTLNGENKSLNTYTDEDPLVFEVFPLGN
NRADGMCYLDDGGVTTNAEDNGKFSVVKVAAEQDGGTETITFTNDCYEYV
FGGPFYVRVRGAQSPSNIHVSSGAGSQDMKVSSATSRAALFNDGENGDFW
VDQETDSLWLKLPNVVLPDAVITIT
Ligand information
Ligand IDNOJ
InChIInChI=1S/C6H13NO4/c8-2-3-5(10)6(11)4(9)1-7-3/h3-11H,1-2H2/t3-,4+,5-,6-/m1/s1
InChIKeyLXBIFEVIBLOUGU-JGWLITMVSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01OC1C(NCC(O)C1O)CO
OpenEye OEToolkits 1.7.0C1C(C(C(C(N1)CO)O)O)O
OpenEye OEToolkits 1.7.0C1[C@@H]([C@H]([C@@H]([C@H](N1)CO)O)O)O
CACTVS 3.370OC[CH]1NC[CH](O)[CH](O)[CH]1O
CACTVS 3.370OC[C@H]1NC[C@H](O)[C@@H](O)[C@@H]1O
FormulaC6 H13 N O4
Name1-DEOXYNOJIRIMYCIN;
MORANOLINE
ChEMBLCHEMBL307429
DrugBankDB03206
ZINCZINC000003794714
PDB chain2x2j Chain A Residue 1050 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2x2j Crystal Structure of Alpha-1,4-Glucan Lyase, a Unique Glycoside Hydrolase Family Member with a Novel Catalytic Mechanism.
Resolution2.35 Å
Binding residue
(original residue number in PDB)		F373 D412 N459 Y513 W551 D553 M554 R649 W662 D665 F698 H731
Binding residue
(residue number reindexed from 1)		F360 D399 N446 Y500 W538 D540 M541 R636 W649 D652 F685 H718
Annotation score1
Enzymatic activity
Enzyme Commision number 4.2.2.13: exo-(1->4)-alpha-D-glucan lyase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016829 lyase activity
GO:0030246 carbohydrate binding
GO:0047457 exo-(1,4)-alpha-D-glucan lyase activity
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2x2j, PDBe:2x2j, PDBj:2x2j
PDBsum2x2j
PubMed23902768
UniProtQ9STC1

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