2JF4

Family 37 trehalase from Escherichia coli in complex with validoxylamine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004555	molecular_function	alpha,alpha-trehalase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0005991	biological_process	trehalose metabolic process
A	0005993	biological_process	trehalose catabolic process
A	0006974	biological_process	DNA damage response
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0042597	cellular_component	periplasmic space
A	0071474	biological_process	cellular hyperosmotic response

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE VDM A1548

Chain	Residue
A	ARG152
A	ARG277
A	GLU279
A	SER280
A	ALA307
A	GLY310
A	ASP312
A	GLN446
A	TRP447
A	GLU511
A	TYR512
A	PHE153
A	PHE518
A	TRP520
A	HOH2178
A	HOH2263
A	TYR157
A	TRP159
A	ASP160
A	ASN196
A	TYR202
A	ARG205
A	GLN207

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Functional Information from PROSITE/UniProt

site_id	PS00927
Number of Residues	14
Details	TREHALASE_1 Trehalase signature 1. PGGRFrEvYyWDsY

Chain	Residue	Details
A	PRO149-TYR162

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site_id	PS00928
Number of Residues	10
Details	TREHALASE_2 Trehalase signature 2. QWDaPnGWAP

Chain	Residue	Details
A	GLN446-PRO455

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17455176","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19123216","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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