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7JTY

Co-crystal structure of alpha glucosidase with compound 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0030246molecular_functioncarbohydrate binding
B0001701biological_processin utero embryonic development
B0001889biological_processliver development
B0003723molecular_functionRNA binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0006491biological_processN-glycan processing
B0010977biological_processnegative regulation of neuron projection development
B0017177cellular_componentglucosidase II complex
B0043231cellular_componentintracellular membrane-bounded organelle
B0044877molecular_functionprotein-containing complex binding
B0046872molecular_functionmetal ion binding
B0071941biological_processnitrogen cycle metabolic process
C0003824molecular_functioncatalytic activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0030246molecular_functioncarbohydrate binding
D0001701biological_processin utero embryonic development
D0001889biological_processliver development
D0003723molecular_functionRNA binding
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005783cellular_componentendoplasmic reticulum
D0006491biological_processN-glycan processing
D0010977biological_processnegative regulation of neuron projection development
D0017177cellular_componentglucosidase II complex
D0043231cellular_componentintracellular membrane-bounded organelle
D0044877molecular_functionprotein-containing complex binding
D0046872molecular_functionmetal ion binding
D0071941biological_processnitrogen cycle metabolic process
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DDNMDGMVSlaEL
ChainResidueDetails
BASP222-LEU234

site_idPS00129
Number of Residues8
DetailsGLYCOSYL_HYDROL_F31_1 Glycosyl hydrolases family 31 active site. YVWnDMNE
ChainResidueDetails
ATYR560-GLU567

site_idPS00707
Number of Residues31
DetailsGLYCOSYL_HYDROL_F31_2 Glycosyl hydrolases family 31 signature 2. GADVGGFfknPepeLLvRWyqMGAYqPFfRA
ChainResidueDetails
AGLY667-ALA697

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10066, ECO:0000269|PubMed:27462106, ECO:0007744|PDB:5HJR
ChainResidueDetails
AASP564
CASP564
DASP49
DASP53

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:27462106
ChainResidueDetails
AASP640
BASP104
BGLU105
DGLN50
DTYR55
DASP57
DASP63
DGLU64
DARG91
DASP94
DVAL96
CASP640
DASP98
DASP104
DGLU105
BASP57
BASP63
BGLU64
BARG91
BASP94
BVAL96
BASP98

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:27462106, ECO:0007744|PDB:5HJO
ChainResidueDetails
AASP305
DGLU233
AASP451
AARG624
AHIS698
CASP305
CASP451
CARG624
CHIS698
DMET228

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q14697
ChainResidueDetails
ASER52
CSER52
DSER24
DSER168

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10921916, ECO:0000269|PubMed:27462106, ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5HJO, ECO:0007744|PDB:5HJR, ECO:0007744|PDB:5IED, ECO:0007744|PDB:5IEE, ECO:0007744|PDB:5IEF, ECO:0007744|PDB:5IEG
ChainResidueDetails
AASP97
CASP97
BSER383
BSER427
DSER89
DSER376
DSER383
DSER427

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
BLYS166
DLYS166

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN72
BASN469
DASN72
DASN469

227344

PDB entries from 2024-11-13

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