Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1ABB

CONTROL OF PHOSPHORYLASE B CONFORMATION BY A MODIFIED COFACTOR: CRYSTALLOGRAPHIC STUDIES ON R-STATE GLYCOGEN PHOSPHORYLASE RECONSTITUTED WITH PYRIDOXAL 5'-DIPHOSPHATE

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	5
Details	BINDING SITE FOR RESIDUE SO4 A 900

Chain	Residue
A	LYS11
A	SER14
A	ARG16
A	ARG69
B	ARG43

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 900

Chain	Residue
B	ARG69
A	ARG43
B	LYS11
B	SER14
B	ARG16

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 900

Chain	Residue
C	LYS11
C	SER14
C	ARG16
C	ARG69
D	ARG43

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 900

Chain	Residue
C	ARG43
D	LYS11
D	SER14
D	ARG16
D	ARG69

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PDP A 931

Chain	Residue
A	ARG138
A	TRP491
A	LYS568
A	ARG569
A	LYS574
A	ARG649
A	VAL650
A	THR676
A	GLY677
A	LYS680

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE IMP A 920

Chain	Residue
A	TRP67
A	GLN71
A	TYR75
A	ARG309
A	ARG310
A	LYS315
B	ASP42
B	ASN44
B	VAL45

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PDP B 932

Chain	Residue
B	TYR90
B	ARG138
B	TRP491
B	LYS568
B	ARG569
B	LYS574
B	ARG649
B	VAL650
B	ALA653
B	THR676
B	GLY677
B	LYS680

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE IMP B 920

Chain	Residue
A	ASP42
A	ASN44
A	VAL45
B	TRP67
B	TYR75
B	GLU76
B	ARG309
B	ARG310
B	LYS315

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PDP C 933

Chain	Residue
C	TRP491
C	LYS568
C	ARG569
C	LYS574
C	TYR648
C	ARG649
C	VAL650
C	ALA653
C	THR676
C	GLY677
C	LYS680

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE IMP C 920

Chain	Residue
C	GLN71
C	TYR75
C	GLU76
C	TYR155
C	ARG309
C	ARG310
C	LYS315
D	ASP42
D	ASN44
D	VAL45

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PDP D 934

Chain	Residue
D	TYR90
D	ARG138
D	TRP491
D	LYS568
D	ARG569
D	LYS574
D	VAL650
D	THR676
D	GLY677
D	LYS680

site_id	BC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE IMP D 920

Chain	Residue
D	GLU76
D	ARG309
D	ARG310
D	LYS315
C	ASP42
C	ASN44
C	VAL45
D	TRP67
D	ILE68
D	GLN71
D	GLN72
D	TYR75

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	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	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	LYS680	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	LYS680	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	LYS680	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	LYS680	covalently attached

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