Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1GPA

STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP

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
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0004645	molecular_function	1,4-alpha-oligoglucan phosphorylase activity
B	0005737	cellular_component	cytoplasm
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	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0098723	cellular_component	skeletal muscle myofibril
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0004645	molecular_function	1,4-alpha-oligoglucan phosphorylase activity
C	0005737	cellular_component	cytoplasm
C	0005975	biological_process	carbohydrate metabolic process
C	0005977	biological_process	glycogen metabolic process
C	0005980	biological_process	glycogen catabolic process
C	0008184	molecular_function	glycogen phosphorylase activity
C	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0098723	cellular_component	skeletal muscle myofibril
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0004645	molecular_function	1,4-alpha-oligoglucan phosphorylase activity
D	0005737	cellular_component	cytoplasm
D	0005975	biological_process	carbohydrate metabolic process
D	0005977	biological_process	glycogen metabolic process
D	0005980	biological_process	glycogen catabolic process
D	0008184	molecular_function	glycogen phosphorylase activity
D	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0098723	cellular_component	skeletal muscle myofibril

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 901

Chain	Residue
A	ARG569
A	TYR573
A	LYS574

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 902

Chain	Residue
A	ARG242
A	ARG310

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 901

Chain	Residue
B	PLP999
B	GLY135
B	ARG569
B	TYR573
B	LYS574

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 902

Chain	Residue
B	ARG242
B	ARG310

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 901

Chain	Residue
C	ARG569
C	TYR573
C	LYS574

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 902

Chain	Residue
C	TYR155
C	ARG242
C	ARG310

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 901

Chain	Residue
D	ARG569
D	TYR573
D	LYS574

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 D 902

Chain	Residue
D	ARG242
D	ARG310

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PLP A 999

Chain	Residue
A	ARG138
A	TRP491
A	LYS568
A	TYR648
A	ARG649
A	VAL650
A	ALA653
A	GLY675
A	THR676
A	GLY677
A	LYS680

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PLP B 999

Chain	Residue
B	TRP491
B	LYS568
B	LYS574
B	TYR648
B	ARG649
B	ALA653
B	GLY675
B	THR676
B	GLY677
B	LYS680
B	SO4901

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PLP C 999

Chain	Residue
C	ARG138
C	TRP491
C	LYS568
C	TYR648
C	ARG649
C	VAL650
C	GLY675
C	THR676
C	GLY677
C	LYS680

site_id	BC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PLP D 999

Chain	Residue
D	TYR90
D	ARG138
D	TRP491
D	LYS568
D	TYR648
D	ARG649
D	VAL650
D	THR676
D	GLY677
D	LYS680

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	40
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P11217","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"3616621","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Site: {"description":"Involved in the association of subunits","evidences":[{"source":"PubMed","id":"728424","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Can be labeled by an AMP analog; may be involved in allosteric regulation","evidences":[{"source":"PubMed","id":"728424","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by PHK; in form phosphorylase A","evidences":[{"source":"UniProtKB","id":"P11217","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P09812","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9WUB3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9WUB3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09812","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"7500360","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8976550","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PRI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2SKC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2SKD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2SKE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 1900534, 6425278, 11886794, 15272305, 12460107

Chain	Residue	Details
A	ARG569
A	LYS568
A	THR676
A	LYS574

site_id	CSA2
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 1900534, 6425278, 11886794, 15272305, 12460107

Chain	Residue	Details
B	ARG569
B	LYS568
B	THR676
B	LYS574

site_id	CSA3
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 1900534, 6425278, 11886794, 15272305, 12460107

Chain	Residue	Details
C	ARG569
C	LYS568
C	THR676
C	LYS574

site_id	CSA4
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 1900534, 6425278, 11886794, 15272305, 12460107

Chain	Residue	Details
D	ARG569
D	LYS568
D	THR676
D	LYS574

site_id	MCSA1
Number of Residues	6
Details	M-CSA 205

Chain	Residue	Details
A	PRO381	electrostatic stabiliser
A	GLU572	electrostatic stabiliser
A	TYR573	electrostatic stabiliser
A	LEU578	electrostatic stabiliser
A	LYS680	electrostatic stabiliser
A	ASN684	covalently attached

site_id	MCSA2
Number of Residues	6
Details	M-CSA 205

Chain	Residue	Details
B	PRO381	electrostatic stabiliser
B	GLU572	electrostatic stabiliser
B	TYR573	electrostatic stabiliser
B	LEU578	electrostatic stabiliser
B	LYS680	electrostatic stabiliser
B	ASN684	covalently attached

site_id	MCSA3
Number of Residues	6
Details	M-CSA 205

Chain	Residue	Details
C	PRO381	electrostatic stabiliser
C	GLU572	electrostatic stabiliser
C	TYR573	electrostatic stabiliser
C	LEU578	electrostatic stabiliser
C	LYS680	electrostatic stabiliser
C	ASN684	covalently attached

site_id	MCSA4
Number of Residues	6
Details	M-CSA 205

Chain	Residue	Details
D	PRO381	electrostatic stabiliser
D	GLU572	electrostatic stabiliser
D	TYR573	electrostatic stabiliser
D	LEU578	electrostatic stabiliser
D	LYS680	electrostatic stabiliser
D	ASN684	covalently attached

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)