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2JG0

Family 37 trehalase from Escherichia coli in complex with 1- thiatrehazolin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004555molecular_functionalpha,alpha-trehalase activity
A0005975biological_processcarbohydrate metabolic process
A0005991biological_processtrehalose metabolic process
A0005993biological_processtrehalose catabolic process
A0006974biological_processDNA damage response
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0071474biological_processcellular hyperosmotic response
Functional Information from PROSITE/UniProt
site_idPS00927
Number of Residues14
DetailsTREHALASE_1 Trehalase signature 1. PGGRFrEvYyWDsY
ChainResidueDetails
APRO149-TYR162

site_idPS00928
Number of Residues10
DetailsTREHALASE_2 Trehalase signature 2. QWDaPnGWAP
ChainResidueDetails
AGLN446-PRO455

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:17455176, ECO:0000305|PubMed:19123216
ChainResidueDetails
AASP312
AGLU496

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AARG152
ATRP159
AASN196
AARG205
AARG277
AGLY310
AGLU511

223166

PDB entries from 2024-07-31

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