Structure of PDB 2wyn Chain B

Receptor sequence

>2wynB (length=503) Species: 83333 (Escherichia coli K-12)

ETPVTPQPPDILLGPLFNDVQNAKLFPDQKTFADAVPNSDPLMILADYRM
QQNQSGFDLRHFVNVNFTLPKYVPPEGQSLREHIDGLWPVLTRSTENTEK
WDSLLPLPEPYVVPGGRFREVYYWDSYFTMLGLAESGHWDKVADMVANFA
HEIDTYGHIPNGNRSYYLSRSQPPFFALMVELLAQHEGDAALKQYLPQMQ
KEYAYWMDGVENLQAGQQEKRVVKLQDGTLLNRYWDDRDTPRPESWVEDI
ATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDNPQQLNTLRTTSIVPV
DLNSLMFKMEKILARASKAAGDNAMANQYETLANARQKGIEKYLWNDQQG
WYADYDLKSHKVRNQLTAAALFPLYVNAAAKDRANKMATATKTHLLQPGG
LNTTSVKSGQQWDAPNGWAPLQWVATEGLQNYGQKEVAMDISWHFLTNVQ
HTYDREKKLVEKYDVSTTYPLQDGFGWTNGVTLKMLDLICPKEQPCDNVP
ATR

3D structure

• PDB: 2wyn Casuarine-6-O-alpha-D-glucoside and its analogues are tight binding inhibitors of insect and bacterial trehalases.
• Chain: B
• Resolution: 2.1 Å

Enzymatic activity

• Enzyme Commision number: 3.2.1.28: alpha,alpha-trehalase.

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	LG9	B	F153 W159 D160 G310 D312 W447 Y512 F518 W520	F118 W124 D125 G275 D277 W412 Y469 F475 W477	PDBbind-CN: -logKd/Ki=5.55,Ki=2.8uM
BS02	GLC	B	R152 Y157 N196 Y202 R205 E279	R117 Y122 N161 Y167 R170 E244	PDBbind-CN: -logKd/Ki=5.55,Ki=2.8uM

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

External links

• PDB: RCSB:2wyn, PDBe:2wyn, PDBj:2wyn
• PDBsum: 2wyn
• PubMed: 20461849
• UniProt: P13482|TREA_ECOLI Periplasmic trehalase (Gene Name=treA)