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4AP6

Crystal structure of human POFUT2 E54A mutant in complex with GDP- fucose

Functional Information from GO Data
ChainGOidnamespacecontents
A0001707biological_processmesoderm formation
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005794cellular_componentGolgi apparatus
A0006004biological_processfucose metabolic process
A0006486biological_processprotein glycosylation
A0008417molecular_functionfucosyltransferase activity
A0010468biological_processregulation of gene expression
A0010717biological_processregulation of epithelial to mesenchymal transition
A0016757molecular_functionglycosyltransferase activity
A0036065biological_processfucosylation
A0036066biological_processprotein O-linked fucosylation
A0046922molecular_functionpeptide-O-fucosyltransferase activity
A0051046biological_processregulation of secretion
A1903334biological_processpositive regulation of protein folding
B0001707biological_processmesoderm formation
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005794cellular_componentGolgi apparatus
B0006004biological_processfucose metabolic process
B0006486biological_processprotein glycosylation
B0008417molecular_functionfucosyltransferase activity
B0010468biological_processregulation of gene expression
B0010717biological_processregulation of epithelial to mesenchymal transition
B0016757molecular_functionglycosyltransferase activity
B0036065biological_processfucosylation
B0036066biological_processprotein O-linked fucosylation
B0046922molecular_functionpeptide-O-fucosyltransferase activity
B0051046biological_processregulation of secretion
B1903334biological_processpositive regulation of protein folding
C0001707biological_processmesoderm formation
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0005794cellular_componentGolgi apparatus
C0006004biological_processfucose metabolic process
C0006486biological_processprotein glycosylation
C0008417molecular_functionfucosyltransferase activity
C0010468biological_processregulation of gene expression
C0010717biological_processregulation of epithelial to mesenchymal transition
C0016757molecular_functionglycosyltransferase activity
C0036065biological_processfucosylation
C0036066biological_processprotein O-linked fucosylation
C0046922molecular_functionpeptide-O-fucosyltransferase activity
C0051046biological_processregulation of secretion
C1903334biological_processpositive regulation of protein folding
D0001707biological_processmesoderm formation
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0005794cellular_componentGolgi apparatus
D0006004biological_processfucose metabolic process
D0006486biological_processprotein glycosylation
D0008417molecular_functionfucosyltransferase activity
D0010468biological_processregulation of gene expression
D0010717biological_processregulation of epithelial to mesenchymal transition
D0016757molecular_functionglycosyltransferase activity
D0036065biological_processfucosylation
D0036066biological_processprotein O-linked fucosylation
D0046922molecular_functionpeptide-O-fucosyltransferase activity
D0051046biological_processregulation of secretion
D1903334biological_processpositive regulation of protein folding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:22588082
ChainResidueDetails
AALA54
BALA54
CALA54
DALA54

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:22588082, ECO:0007744|PDB:4AP6
ChainResidueDetails
APRO53
CHIS292
CASP371
CTHR388
DPRO53
DHIS292
DASP371
DTHR388
AHIS292
AASP371
ATHR388
BPRO53
BHIS292
BASP371
BTHR388
CPRO53

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Essential for catalytic activity => ECO:0000269|PubMed:17395589, ECO:0000269|PubMed:22588082
ChainResidueDetails
AGLU396
BGLU396
CGLU396
DGLU396

site_idSWS_FT_FI4
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22588082
ChainResidueDetails
AASN189
AASN259
BASN189
BASN259
CASN189
CASN259
DASN189
DASN259

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN209
BASN209
CASN209
DASN209

222624

PDB entries from 2024-07-17

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