8ZGH

Human lysine O-link glycosylation complex, LH3/ColGalT1 in its apo state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0008475	molecular_function	procollagen-lysine 5-dioxygenase activity
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0031418	molecular_function	L-ascorbic acid binding
B	0005506	molecular_function	iron ion binding
B	0008475	molecular_function	procollagen-lysine 5-dioxygenase activity
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0031418	molecular_function	L-ascorbic acid binding
C	0005506	molecular_function	iron ion binding
C	0008475	molecular_function	procollagen-lysine 5-dioxygenase activity
C	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C	0031418	molecular_function	L-ascorbic acid binding
D	0005506	molecular_function	iron ion binding
D	0008475	molecular_function	procollagen-lysine 5-dioxygenase activity
D	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D	0031418	molecular_function	L-ascorbic acid binding
U	0005788	cellular_component	endoplasmic reticulum lumen
U	0016020	cellular_component	membrane
U	0030199	biological_process	collagen fibril organization
U	0050211	molecular_function	procollagen galactosyltransferase activity
U	0180062	biological_process	protein O-linked glycosylation via galactose
U	1904028	biological_process	positive regulation of collagen fibril organization
V	0005788	cellular_component	endoplasmic reticulum lumen
V	0016020	cellular_component	membrane
V	0030199	biological_process	collagen fibril organization
V	0050211	molecular_function	procollagen galactosyltransferase activity
V	0180062	biological_process	protein O-linked glycosylation via galactose
V	1904028	biological_process	positive regulation of collagen fibril organization
W	0005788	cellular_component	endoplasmic reticulum lumen
W	0016020	cellular_component	membrane
W	0030199	biological_process	collagen fibril organization
W	0050211	molecular_function	procollagen galactosyltransferase activity
W	0180062	biological_process	protein O-linked glycosylation via galactose
W	1904028	biological_process	positive regulation of collagen fibril organization
X	0005788	cellular_component	endoplasmic reticulum lumen
X	0016020	cellular_component	membrane
X	0030199	biological_process	collagen fibril organization
X	0050211	molecular_function	procollagen galactosyltransferase activity
X	0180062	biological_process	protein O-linked glycosylation via galactose
X	1904028	biological_process	positive regulation of collagen fibril organization

Functional Information from PROSITE/UniProt

site_id	PS01325
Number of Residues	8
Details	LYS_HYDROXYLASE Lysyl hydroxylase signature. PHHDSSTF

Chain	Residue	Details
A	PRO666-PHE673

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	364
Details	Domain: {"description":"Fe2OG dioxygenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	900
Details	Region: {"description":"Accessory region","evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	172
Details	Region: {"description":"Important for dimerization","evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	56
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FXY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FXY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"30089812","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6FXY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	136
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	12
Details	Motif: {"description":"Endoplasmic reticulum retention motif","evidences":[{"source":"PubMed","id":"20470363","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	72
Details	Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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