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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
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
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
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
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
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250
ChainResidueDetails
AALA380
AGLU580
BALA380
BGLU580
CALA380
CGLU580
DALA380
DGLU580

site_idSWS_FT_FI2
Number of Residues36
DetailsBINDING: BINDING => ECO:0000269|Ref.13, ECO:0007744|PDB:7EAW
ChainResidueDetails
AARG224
BARG224
BASP232
BASN268
BARG277
BGLN279
BARG344
BGLU346
BGLU580
BGLU595
CARG224
AASP232
CASP232
CASN268
CARG277
CGLN279
CARG344
CGLU346
CGLU580
CGLU595
DARG224
DASP232
AASN268
DASN268
DARG277
DGLN279
DARG344
DGLU346
DGLU580
DGLU595
AARG277
AGLN279
AARG344
AGLU346
AGLU580
AGLU595

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PDB entries from 2024-10-30

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