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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8ZGC

Human lysine O-link glycosylation complex, LH3/ColGalT1 with bound UDP-galactose

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0008475molecular_functionprocollagen-lysine 5-dioxygenase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0031418molecular_functionL-ascorbic acid binding
B0005506molecular_functioniron ion binding
B0008475molecular_functionprocollagen-lysine 5-dioxygenase activity
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0031418molecular_functionL-ascorbic acid binding
C0005506molecular_functioniron ion binding
C0008475molecular_functionprocollagen-lysine 5-dioxygenase activity
C0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C0031418molecular_functionL-ascorbic acid binding
D0005506molecular_functioniron ion binding
D0008475molecular_functionprocollagen-lysine 5-dioxygenase activity
D0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D0031418molecular_functionL-ascorbic acid binding
U0005788cellular_componentendoplasmic reticulum lumen
U0016020cellular_componentmembrane
U0016740molecular_functiontransferase activity
U0016757molecular_functionglycosyltransferase activity
U0030199biological_processcollagen fibril organization
U0050211molecular_functionprocollagen galactosyltransferase activity
U0180062biological_processprotein O-linked glycosylation via galactose
U1904028biological_processpositive regulation of collagen fibril organization
V0005788cellular_componentendoplasmic reticulum lumen
V0016020cellular_componentmembrane
V0016740molecular_functiontransferase activity
V0016757molecular_functionglycosyltransferase activity
V0030199biological_processcollagen fibril organization
V0050211molecular_functionprocollagen galactosyltransferase activity
V0180062biological_processprotein O-linked glycosylation via galactose
V1904028biological_processpositive regulation of collagen fibril organization
W0005788cellular_componentendoplasmic reticulum lumen
W0016020cellular_componentmembrane
W0016740molecular_functiontransferase activity
W0016757molecular_functionglycosyltransferase activity
W0030199biological_processcollagen fibril organization
W0050211molecular_functionprocollagen galactosyltransferase activity
W0180062biological_processprotein O-linked glycosylation via galactose
W1904028biological_processpositive regulation of collagen fibril organization
X0005788cellular_componentendoplasmic reticulum lumen
X0016020cellular_componentmembrane
X0016740molecular_functiontransferase activity
X0016757molecular_functionglycosyltransferase activity
X0030199biological_processcollagen fibril organization
X0050211molecular_functionprocollagen galactosyltransferase activity
X0180062biological_processprotein O-linked glycosylation via galactose
X1904028biological_processpositive regulation of collagen fibril organization
Functional Information from PROSITE/UniProt
site_idPS01325
Number of Residues8
DetailsLYS_HYDROXYLASE Lysyl hydroxylase signature. PHHDSSTF
ChainResidueDetails
APRO666-PHE673
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues364
DetailsDomain: {"description":"Fe2OG dioxygenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues900
DetailsRegion: {"description":"Accessory region","evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues172
DetailsRegion: {"description":"Important for dimerization","evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues56
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FXY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FXY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FXY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues136
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues12
DetailsMotif: {"description":"Endoplasmic reticulum retention motif","evidences":[{"source":"PubMed","id":"20470363","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues72
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-01-21

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