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5IEE

Murine endoplasmic reticulum alpha-glucosidase II with 1-deoxynojirimycin

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0030246molecular_functioncarbohydrate binding
Functional Information from PROSITE/UniProt
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
DetailsBINDING: BINDING => ECO:0000269|PubMed:27462106, ECO:0007744|PDB:5HJO
ChainResidueDetails
BASP49
BASP53

site_idSWS_FT_FI2
Number of Residues11
DetailsBINDING: BINDING => ECO:0000269|PubMed:27462106, ECO:0007744|PDB:5F0E, ECO:0007744|PDB:5H9O, 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
BGLU64
BARG91
BASP94
BVAL96
BASP98
BASP104
BGLU105
BGLN50
BTYR55
BASP57
BASP63

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000255
ChainResidueDetails
BSER89
AASP451
AARG624
AHIS698

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN72

site_idSWS_FT_FI5
Number of Residues1
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
AASN97

220472

PDB entries from 2024-05-29

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