1Z8D

Crystal Structure of Human Muscle Glycogen Phosphorylase a with AMP and Glucose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0004645	molecular_function	1,4-alpha-oligoglucan phosphorylase activity
A	0005515	molecular_function	protein binding
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	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0070062	cellular_component	extracellular exosome

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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:16523484, ECO:0007744|PDB:1Z8D

Chain	Residue	Details
A	ASP42
A	TYR75
A	ARG309

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site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Involved in the association of subunits => ECO:0000250|UniProtKB:P00489

Chain	Residue	Details
A	CYS108
A	CYS142

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site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: May be involved in allosteric control => ECO:0000250|UniProtKB:P00489

Chain	Residue	Details
A	TYR155

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P00489

Chain	Residue	Details
A	SER1

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PHK; in form phosphorylase A => ECO:0000269|PubMed:1150650

Chain	Residue	Details
A	SEP14

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site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09812

Chain	Residue	Details
A	TYR203
A	TYR226

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3

Chain	Residue	Details
A	SER429

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3

Chain	Residue	Details
A	TYR472

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site_id	SWS_FT_FI9
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09812

Chain	Residue	Details
A	SER513
A	SER746
A	SER747

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site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:P00489

Chain	Residue	Details
A	LLP680

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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

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