Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8CVZ

Human glycogenin-1 and glycogen synthase-1 complex in the apo ordered state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004373	molecular_function	alpha-1,4-glucan glucosyltransferase (UDP-glucose donor) activity
A	0005978	biological_process	glycogen biosynthetic process
B	0004373	molecular_function	alpha-1,4-glucan glucosyltransferase (UDP-glucose donor) activity
B	0005978	biological_process	glycogen biosynthetic process
C	0004373	molecular_function	alpha-1,4-glucan glucosyltransferase (UDP-glucose donor) activity
C	0005978	biological_process	glycogen biosynthetic process
D	0004373	molecular_function	alpha-1,4-glucan glucosyltransferase (UDP-glucose donor) activity
D	0005978	biological_process	glycogen biosynthetic process
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005978	biological_process	glycogen biosynthetic process
E	0008466	molecular_function	glycogenin glucosyltransferase activity
E	0016020	cellular_component	membrane
E	0016740	molecular_function	transferase activity
E	0016757	molecular_function	glycosyltransferase activity
E	0030145	molecular_function	manganese ion binding
E	0034774	cellular_component	secretory granule lumen
E	0042803	molecular_function	protein homodimerization activity
E	0043202	cellular_component	lysosomal lumen
E	0046872	molecular_function	metal ion binding
E	1904813	cellular_component	ficolin-1-rich granule lumen
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005978	biological_process	glycogen biosynthetic process
F	0008466	molecular_function	glycogenin glucosyltransferase activity
F	0016020	cellular_component	membrane
F	0016740	molecular_function	transferase activity
F	0016757	molecular_function	glycosyltransferase activity
F	0030145	molecular_function	manganese ion binding
F	0034774	cellular_component	secretory granule lumen
F	0042803	molecular_function	protein homodimerization activity
F	0043202	cellular_component	lysosomal lumen
F	0046872	molecular_function	metal ion binding
F	1904813	cellular_component	ficolin-1-rich granule lumen
G	0005515	molecular_function	protein binding
G	0005576	cellular_component	extracellular region
G	0005634	cellular_component	nucleus
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0005978	biological_process	glycogen biosynthetic process
G	0008466	molecular_function	glycogenin glucosyltransferase activity
G	0016020	cellular_component	membrane
G	0016740	molecular_function	transferase activity
G	0016757	molecular_function	glycosyltransferase activity
G	0030145	molecular_function	manganese ion binding
G	0034774	cellular_component	secretory granule lumen
G	0042803	molecular_function	protein homodimerization activity
G	0043202	cellular_component	lysosomal lumen
G	0046872	molecular_function	metal ion binding
G	1904813	cellular_component	ficolin-1-rich granule lumen
H	0005515	molecular_function	protein binding
H	0005576	cellular_component	extracellular region
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0005978	biological_process	glycogen biosynthetic process
H	0008466	molecular_function	glycogenin glucosyltransferase activity
H	0016020	cellular_component	membrane
H	0016740	molecular_function	transferase activity
H	0016757	molecular_function	glycosyltransferase activity
H	0030145	molecular_function	manganese ion binding
H	0034774	cellular_component	secretory granule lumen
H	0042803	molecular_function	protein homodimerization activity
H	0043202	cellular_component	lysosomal lumen
H	0046872	molecular_function	metal ion binding
H	1904813	cellular_component	ficolin-1-rich granule lumen
I	0005515	molecular_function	protein binding
I	0005576	cellular_component	extracellular region
I	0005634	cellular_component	nucleus
I	0005737	cellular_component	cytoplasm
I	0005829	cellular_component	cytosol
I	0005978	biological_process	glycogen biosynthetic process
I	0008466	molecular_function	glycogenin glucosyltransferase activity
I	0016020	cellular_component	membrane
I	0016740	molecular_function	transferase activity
I	0016757	molecular_function	glycosyltransferase activity
I	0030145	molecular_function	manganese ion binding
I	0034774	cellular_component	secretory granule lumen
I	0042803	molecular_function	protein homodimerization activity
I	0043202	cellular_component	lysosomal lumen
I	0046872	molecular_function	metal ion binding
I	1904813	cellular_component	ficolin-1-rich granule lumen
J	0005515	molecular_function	protein binding
J	0005576	cellular_component	extracellular region
J	0005634	cellular_component	nucleus
J	0005737	cellular_component	cytoplasm
J	0005829	cellular_component	cytosol
J	0005978	biological_process	glycogen biosynthetic process
J	0008466	molecular_function	glycogenin glucosyltransferase activity
J	0016020	cellular_component	membrane
J	0016740	molecular_function	transferase activity
J	0016757	molecular_function	glycosyltransferase activity
J	0030145	molecular_function	manganese ion binding
J	0034774	cellular_component	secretory granule lumen
J	0042803	molecular_function	protein homodimerization activity
J	0043202	cellular_component	lysosomal lumen
J	0046872	molecular_function	metal ion binding
J	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22160680","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3RMW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3T7O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P13280","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22160680","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3T7O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"3RMW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3T7O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P13280","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N-acetylthreonine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P13280","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (Glc...) tyrosine","evidences":[{"source":"PubMed","id":"22160680","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30356213","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3U2U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3U2V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35835870","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7Q13","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35835870","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7Q13","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"35835870","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7Q13","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35835870","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7Q12","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7Q13","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"35690592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)