Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3E3N

The Glycogen phosphorylase b R state- AMP complex

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE AMP A 843

Chain	Residue
A	TRP67
A	HOH887
B	ASP42
B	ASN44
B	VAL45
A	GLN71
A	TYR75
A	ARG309
A	ARG310
A	LYS315
A	PHE316
A	GLY317
A	CYS318

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 844

Chain	Residue
A	SER14
A	ARG16
A	ARG69
A	HOH867
B	ARG43

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 845

Chain	Residue
A	GLY135
A	ARG569
A	LYS574
A	HOH849

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE AMP B 843

Chain	Residue
A	ASP42
A	ASN44
A	VAL45
B	TRP67
B	GLN71
B	TYR75
B	ARG309
B	ARG310
B	LYS315
B	PHE316
B	GLY317
B	CYS318
B	HOH863

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 844

Chain	Residue
A	ARG43
B	SER14
B	ARG16
B	ARG69

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 845

Chain	Residue
B	GLY134
B	GLY135
B	ARG569
B	LYS574

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP C 843

Chain	Residue
C	TRP67
C	GLN71
C	TYR75
C	ARG309
C	ARG310
D	ASP42
D	ASN44
D	VAL45

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 844

Chain	Residue
C	GLY135
C	ARG569
C	LYS574
C	LLP680

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 845

Chain	Residue
C	ARG43
D	SER14
D	ARG16
D	ARG69

site_id	BC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE AMP D 843

Chain	Residue
C	ASP42
C	ASN44
C	VAL45
D	TRP67
D	GLN71
D	TYR75
D	ARG309
D	ARG310
D	LYS315
D	GLY317
D	CYS318
D	HOH876
D	HOH908

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 844

Chain	Residue
C	SER14
C	ARG16
C	ARG69
D	ARG43

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 845

Chain	Residue
D	GLY135
D	ARG569
D	LYS574
D	LLP680

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AMP E 843

Chain	Residue
E	TRP67
E	GLN71
E	TYR75
E	ARG309
E	ARG310
F	ASP42
F	ASN44
F	VAL45

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 844

Chain	Residue
E	SER14
E	ARG16
E	ARG69
E	HOH863
F	ARG43

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 845

Chain	Residue
E	GLY135
E	ARG569
E	LLP680

site_id	BC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AMP F 843

Chain	Residue
F	GLN71
F	TYR75
F	ARG309
F	ARG310
F	LYS315
F	PHE316
F	GLY317
F	CYS318
F	HOH854
E	ASP42
E	ASN44
E	VAL45

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 F 844

Chain	Residue
E	ARG43
F	LYS11
F	SER14
F	ARG16
F	ARG69

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 F 845

Chain	Residue
F	GLY135
F	ARG569
F	LYS574
F	LLP680
F	HOH879

site_id	CC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AMP G 843

Chain	Residue
G	TRP67
G	GLN71
G	TYR75
G	ARG309
G	ARG310
G	LYS315
G	PHE316
G	GLY317
G	CYS318
G	HOH866
H	ASP42
H	ASN44

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 G 844

Chain	Residue
G	SER14
G	ARG16
G	ARG69
H	ARG43

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 G 845

Chain	Residue
G	GLY135
G	ARG569
G	LYS574
G	LLP680

site_id	CC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE AMP H 843

Chain	Residue
G	ASP42
G	ASN44
G	VAL45
H	TRP67
H	GLN71
H	TYR75
H	ARG309
H	ARG310
H	LYS315
H	PHE316
H	GLY317
H	CYS318

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 H 844

Chain	Residue
G	ARG43
H	LYS11
H	SER14
H	ARG69

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 H 899

Chain	Residue
H	ASN133
H	GLY135
H	ARG569

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	62
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P11217","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"3616621","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
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	8
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	8
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	16
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P09812","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9WUB3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9WUB3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	24
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09812","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
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	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	ARG569
B	LYS568
B	THR676
B	LYS574

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1gpa

Chain	Residue	Details
C	ARG569
C	LYS568
C	THR676
C	LYS574

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1gpa

Chain	Residue	Details
D	ARG569
D	LYS568
D	THR676
D	LYS574

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1gpa

Chain	Residue	Details
E	ARG569
E	LYS568
E	THR676
E	LYS574

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1gpa

Chain	Residue	Details
F	ARG569
F	LYS568
F	THR676
F	LYS574

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1gpa

Chain	Residue	Details
G	ARG569
G	LYS568
G	THR676
G	LYS574

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1gpa

Chain	Residue	Details
H	ARG569
H	LYS568
H	THR676
H	LYS574

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

site_id	MCSA2
Number of Residues	6
Details	M-CSA 205

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

site_id	MCSA3
Number of Residues	6
Details	M-CSA 205

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

site_id	MCSA4
Number of Residues	6
Details	M-CSA 205

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

site_id	MCSA5
Number of Residues	6
Details	M-CSA 205

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

site_id	MCSA6
Number of Residues	6
Details	M-CSA 205

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

site_id	MCSA7
Number of Residues	6
Details	M-CSA 205

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

site_id	MCSA8
Number of Residues	6
Details	M-CSA 205

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)