Structure of PDB 2jjb Chain A Binding Site BS01

Receptor Information
>2jjb Chain A (length=504) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VTPQPPDILLGPLFNDVQNAKLFPDQKTFADAVPNSDPLMILADYRMQQN
QFDLRHFVNVNFTLPKYVPPEGQSLREHIDGLWPVLTRSTENTEKWDSLL
PLPEPYVVPGGRFREVYYWDSYFTMLGLAESGHWDKVADMVANFAHEIDT
YGHIPNGNRSYYLSRSQPPFFALMVELLAQHEGDAALKQYLPQMQKEYAY
WMDGVENLQAGQQEKRVVKLQDGTLLNRYWDDRDTPRPESWVEDIATAKS
NPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLNTLRTTSIVPVDLNSL
MFKMEKILARASKAAGDNAMANQYETLANARQKGIEKYLWNDQQGWYADY
DLKSHKVRNQLTAAALFPLYVNAAAKDRANKMATATKTHLLQPGGLNTTS
VKSGQQWDAPNGWAPLQWVATEGLQNYGQKEVAMDISWHFLTNVQHTYDR
EKKLVEKYDVSTTGTGGGEYPLQDGFGWTNGVTLKMLDLICPKEQPCDNV
PATR
Ligand information
Ligand ID3CU
InChIInChI=1S/C8H15NO5/c10-2-3-6(12)8(14)5-7(13)4(11)1-9(3)5/h3-8,10-14H,1-2H2/t3-,4+,5-,6-,7-,8-/m1/s1
InChIKeyAXTGOJVKRHFYBT-XAZAIFFQSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1[C@@H]([C@H]([C@H]2[N@@]1[C@@H]([C@H]([C@@H]2O)O)CO)O)O
CACTVS 3.341OC[CH]1[CH](O)[CH](O)[CH]2[CH](O)[CH](O)CN12
CACTVS 3.341OC[C@@H]1[C@@H](O)[C@H](O)[C@H]2[C@H](O)[C@@H](O)CN12
OpenEye OEToolkits 1.5.0C1C(C(C2N1C(C(C2O)O)CO)O)O
ACDLabs 10.04OC2C(O)C1N(C(C(O)C1O)CO)C2
FormulaC8 H15 N O5
NameCASUARINE;
(1R,2R,3R,6S,7S,7aR)-3-(hydroxymethyl)hexahydro-1H-pyrrolizine-1,2,6,7-tetrol
ChEMBLCHEMBL1230107
DrugBank
ZINC
PDB chain2jjb Chain A Residue 1547 [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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PDB2jjb Total Syntheses of Casuarine and its 6-O-Alpha-Glucoside: Complementary Inhibition Towards Glycoside Hydrolases of the Gh31 and Gh37 Families.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		F153 W159 D160 G310 D312 W447 F518 W520
Binding residue
(residue number reindexed from 1)		F113 W119 D120 G270 D272 W407 F476 W478
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.92,Ki=12nM
Enzymatic activity
Enzyme Commision number 3.2.1.28: alpha,alpha-trehalase.
Gene Ontology
Molecular Function
GO:0004555 alpha,alpha-trehalase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0005991 trehalose metabolic process
GO:0005993 trehalose catabolic process
GO:0006974 DNA damage response
GO:0071474 cellular hyperosmotic response
Cellular Component
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2jjb, PDBe:2jjb, PDBj:2jjb
PDBsum2jjb
PubMed19123216
UniProtP13482|TREA_ECOLI Periplasmic trehalase (Gene Name=treA)

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