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7E9X

Trehalase of Arabidopsis thaliana acid mutant -D380A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004555molecular_functionalpha,alpha-trehalase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0005975biological_processcarbohydrate metabolic process
A0005991biological_processtrehalose metabolic process
A0005993biological_processtrehalose catabolic process
A0015927molecular_functiontrehalase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0004555molecular_functionalpha,alpha-trehalase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0005975biological_processcarbohydrate metabolic process
B0005991biological_processtrehalose metabolic process
B0005993biological_processtrehalose catabolic process
B0015927molecular_functiontrehalase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0004555molecular_functionalpha,alpha-trehalase activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005886cellular_componentplasma membrane
C0005975biological_processcarbohydrate metabolic process
C0005991biological_processtrehalose metabolic process
C0005993biological_processtrehalose catabolic process
C0015927molecular_functiontrehalase activity
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0004555molecular_functionalpha,alpha-trehalase activity
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005886cellular_componentplasma membrane
D0005975biological_processcarbohydrate metabolic process
D0005991biological_processtrehalose metabolic process
D0005993biological_processtrehalose catabolic process
D0015927molecular_functiontrehalase activity
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue GOL A 701
ChainResidue
APHE225
ATYR229
ATRP231
AASP232
AGLN279
APHE602
AGOL702
AHOH825

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 702
ChainResidue
ATYR274
AARG277
AARG344
AGLU346
AGOL701
AHOH806
AHOH954
AASN268

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL B 701
ChainResidue
BTRP231
BASP232
BGLN279
BGLU580
BPHE602
BHOH883

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL B 702
ChainResidue
BTYR229
BASN268
BTYR274
BARG277
BARG344
BGLU346
BHOH804
BHOH813

site_idAC5
Number of Residues10
Detailsbinding site for residue GOL C 701
ChainResidue
CPHE225
CTYR229
CASN268
CTYR274
CARG277
CARG344
CGLU346
CGOL702
CHOH825
CHOH876

site_idAC6
Number of Residues9
Detailsbinding site for residue GOL C 702
ChainResidue
CPHE225
CTYR229
CTRP231
CASP232
CGLN279
CPHE602
CTRP604
CGOL701
CHOH833

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL D 701
ChainResidue
DASN268
DARG277
DARG344
DGLU346
DALA375
DGOL702
DHOH842

site_idAC8
Number of Residues7
Detailsbinding site for residue GOL D 702
ChainResidue
DTYR229
DTRP231
DASP232
DGLN279
DGOL701
DHOH814
DHOH955

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues13
DetailsLIPOCALIN Lipocalin signature. EWAr.EVHGLWRNL
ChainResidueDetails
AGLU182-LEU194

site_idPS00928
Number of Residues10
DetailsTREHALASE_2 Trehalase signature 2. QWDsPnGWAP
ChainResidueDetails
AGLN527-PRO536

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2021","submissionDatabase":"PDB data bank","title":"pH-dependent alteration of substrate specificity of plant trehalase and its molecular mechanism.","authors":["Taguchi Y.","Saburi W.","Yu J.","Imai R.","Yao M.","Mori H."]}},{"source":"PDB","id":"7EAW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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