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5N6N

CRYSTAL STRUCTURE OF THE 14-3-3:NEUTRAL TREHALASE NTH1 COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
C0004555molecular_functionalpha,alpha-trehalase activity
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005975biological_processcarbohydrate metabolic process
C0005991biological_processtrehalose metabolic process
C0005993biological_processtrehalose catabolic process
C0015927molecular_functiontrehalase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0046872molecular_functionmetal ion binding
C0071465biological_processcellular response to desiccation
Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG43-VAL53

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
ATYR216-SER235

site_idPS00927
Number of Residues14
DetailsTREHALASE_1 Trehalase signature 1. PGGRFnElYgWDsY
ChainResidueDetails
CPRO299-TYR312

site_idPS00928
Number of Residues10
DetailsTREHALASE_2 Trehalase signature 2. QWDyPfGWAP
ChainResidueDetails
CGLN623-PRO632

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:29087344, ECO:0007744|PDB:5M4A
ChainResidueDetails
CASP478
CGLU674
BGLU136
BGLU185

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:29087344, ECO:0007744|PDB:5N6N
ChainResidueDetails
CASP114
CASP116
CASN118
CGLN120
CASP125

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13482
ChainResidueDetails
CARG302
BSER89

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:29087344, ECO:0007744|PDB:5M4A, ECO:0007744|PDB:5N6N
ChainResidueDetails
CTRP309
CASN346
CARG355
CGLU424
CARG473
CGLY476

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: BMH1 binding => ECO:0000269|PubMed:29087344, ECO:0007744|PDB:5N6N
ChainResidueDetails
CARG55

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378
ChainResidueDetails
CSER2

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:22320399, ECO:0007744|PubMed:19779198
ChainResidueDetails
CSER20
CSER21

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
CSER23

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
ChainResidueDetails
CTHR58

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:22320399, ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
ChainResidueDetails
CSEP60

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
CSER66

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:22320399, ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
CSEP83

223166

PDB entries from 2024-07-31

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