6Y5O

The crystal structure of glycogen phosphorylase in complex with 20

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	0005737	cellular_component	cytoplasm
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	0098723	cellular_component	skeletal muscle myofibril

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue O9Z A 901

Chain	Residue
A	ASN284
A	HOH1094
A	PHE285
A	GLU382
A	HIS571
A	ALA610
A	GLY612
A	TYR613
A	ARG770
A	PHE771

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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	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P11217

Chain	Residue	Details
A	ASP42
A	ARG309

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:3616621

Chain	Residue	Details
A	TYR75

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Involved in the association of subunits => ECO:0000303|PubMed:728424

Chain	Residue	Details
A	CYS108
A	CYS142

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424

Chain	Residue	Details
A	TYR155

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N-acetylserine => ECO:0000269|PubMed:3015680

Chain	Residue	Details
A	SER1

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217

Chain	Residue	Details
A	SER14

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site_id	SWS_FT_FI7
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_FI8
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_FI9
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_FI10
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_FI11
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7500360, ECO:0000269|PubMed:8976550, ECO:0007744|PDB:2PRI, ECO:0007744|PDB:2SKC, ECO:0007744|PDB:2SKD, ECO:0007744|PDB:2SKE

Chain	Residue	Details
A	LLP680

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 205

Chain	Residue	Details
A	HIS377	electrostatic stabiliser
A	LYS568	electrostatic stabiliser
A	ARG569	electrostatic stabiliser
A	LYS574	electrostatic stabiliser
A	THR676	electrostatic stabiliser
A	LLP680	covalently attached

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