1FC0

HUMAN LIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0002060	molecular_function	purine nucleobase binding
A	0003824	molecular_function	catalytic activity
A	0004645	molecular_function	1,4-alpha-oligoglucan phosphorylase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005536	molecular_function	D-glucose binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0005977	biological_process	glycogen metabolic process
A	0005980	biological_process	glycogen catabolic process
A	0008184	molecular_function	glycogen phosphorylase activity
A	0009617	biological_process	response to bacterium
A	0016208	molecular_function	AMP binding
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0019842	molecular_function	vitamin binding
A	0030170	molecular_function	pyridoxal phosphate binding
A	0032052	molecular_function	bile acid binding
A	0034774	cellular_component	secretory granule lumen
A	0042593	biological_process	glucose homeostasis
A	0042802	molecular_function	identical protein binding
A	0070062	cellular_component	extracellular exosome
A	0070266	biological_process	necroptotic process
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0000166	molecular_function	nucleotide binding
B	0002060	molecular_function	purine nucleobase binding
B	0003824	molecular_function	catalytic activity
B	0004645	molecular_function	1,4-alpha-oligoglucan phosphorylase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005536	molecular_function	D-glucose binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0005977	biological_process	glycogen metabolic process
B	0005980	biological_process	glycogen catabolic process
B	0008184	molecular_function	glycogen phosphorylase activity
B	0009617	biological_process	response to bacterium
B	0016208	molecular_function	AMP binding
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0019842	molecular_function	vitamin binding
B	0030170	molecular_function	pyridoxal phosphate binding
B	0032052	molecular_function	bile acid binding
B	0034774	cellular_component	secretory granule lumen
B	0042593	biological_process	glucose homeostasis
B	0042802	molecular_function	identical protein binding
B	0070062	cellular_component	extracellular exosome
B	0070266	biological_process	necroptotic process
B	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PROSITE/UniProt

site_id	PS00102
Number of Residues	13
Details	PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN

Chain	Residue	Details
A	GLU672-ASN684

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10949035","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FA9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Site: {"description":"Involved in the association of subunits","evidences":[{"source":"UniProtKB","id":"P00489","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"May be involved in allosteric control","evidences":[{"source":"UniProtKB","id":"P00489","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9ET01","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22225877","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9ET01","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09811","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10949035","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10980448","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12204691","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EM6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EXV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FA9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FC0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L5Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L5R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L5S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L7X","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1gpa

Chain	Residue	Details
A	ARG569
A	LYS568
A	THR676
A	LYS574

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1gpa

Chain	Residue	Details
B	LYS1574
B	THR1676
B	ARG1569
B	LYS1568

---