3MS2

Glycogen phosphorylase complexed with 4-methylbenzaldehyde-4-(beta-D-glucopyranosyl) thiosemicarbazone

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	11
Details	BINDING SITE FOR RESIDUE 18S A 920

Chain	Residue
A	THR38
A	HOH1044
A	HOH1046
A	VAL40
A	ARG60
A	VAL64
A	GLU190
A	LYS191
A	ALA192
A	TYR226
A	PRO229

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site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 18S A 998

Chain	Residue
A	GLU88
A	ASN133
A	GLY135
A	LEU136
A	TYR280
A	ASN282
A	ASP283
A	HIS341
A	HIS377
A	VAL455
A	ASN484
A	TYR573
A	GLU672
A	ALA673
A	SER674
A	GLY675
A	HOH869
A	HOH877
A	HOH948
A	HOH1012
A	HOH1013

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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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