8CVX

Human glycogenin-1 and glycogen synthase-1 complex in the presence of glucose-6-phosphate

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	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	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	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	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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O

Chain	Residue	Details
E	LEU9
D	HIS297
D	LYS301
D	THR515
C	LYS39
C	HIS297
C	LYS301
C	THR515
H	LEU9
G	LEU9
F	LEU9
B	LYS39
B	HIS297
B	LYS301
B	THR515
D	LYS39

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N, ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X

Chain	Residue	Details
E	ARG77
B	GLU510
B	TRP512
B	GLY513
D	HIS205
D	ARG211
D	ARG331
D	GLU510
D	TRP512
D	GLY513
C	HIS205
H	ARG77
C	ARG211
C	ARG331
C	GLU510
C	TRP512
C	GLY513
G	ARG77
F	ARG77
A	TRP512
A	GLY513
B	HIS205
B	ARG211
B	ARG331

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3QVB, ECO:0007744|PDB:3RMV, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N, ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2T, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X

Chain	Residue	Details
E	ASP102
F	ASP102
F	ASP104
F	HIS212
E	ASP104
E	HIS212
H	ASP102
H	ASP104
H	HIS212
G	ASP102
G	ASP104
G	HIS212

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O

Chain	Residue	Details
E	ASN133
D	HIS501
D	ARG582
D	ARG586
C	GLN294
C	HIS501
C	ARG582
C	ARG586
E	ASP160
H	ASN133
H	ASP160
G	ASN133
G	ASP160
F	ASN133
F	ASP160
D	GLN294

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P13280

Chain	Residue	Details
E	LYS86
H	LYS86
G	LYS86
F	LYS86

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895

Chain	Residue	Details
E	THR2
H	THR2
G	THR2
F	THR2

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13280

Chain	Residue	Details
E	SER44
H	SER44
G	SER44
F	SER44

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	CARBOHYD: O-linked (Glc...) tyrosine => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V

Chain	Residue	Details
E	PHE195
H	PHE195
G	PHE195
F	PHE195

---