Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1NOI

COMPLEX OF GLYCOGEN PHOSPHORYLASE WITH A TRANSITION STATE ANALOGUE NOJIRIMYCIN TETRAZOLE AND PHOSPHATE IN THE T AND R STATES

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	10
Details	BINDING SITE FOR RESIDUE PO4 A 997

Chain	Residue
A	GLY135
A	HOH1063
A	LEU136
A	ARG569
A	TYR573
A	LYS574
A	NTZ998
A	PLP999
A	HOH1013
A	HOH1043

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 B 997

Chain	Residue
B	GLY134
B	GLY135
B	ARG569
B	TYR573
B	LYS574
B	NTZ998
B	PLP999
B	HOH1022
B	HOH1052
B	HOH1072

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 C 997

Chain	Residue
C	GLY135
C	LEU136
C	ARG569
C	TYR573
C	LYS574
C	GLU672
C	NTZ998
C	PLP999
C	HOH1013
C	HOH1044
C	HOH1063

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 D 997

Chain	Residue
D	GLY134
D	GLY135
D	LEU136
D	ARG569
D	TYR573
D	LYS574
D	NTZ998
D	PLP999
D	HOH1023
D	HOH1053
D	HOH1073

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP A 999

Chain	Residue
A	TRP491
A	LYS568
A	LYS574
A	TYR648
A	ARG649
A	VAL650
A	ALA653
A	GLY675
A	THR676
A	GLY677
A	LYS680
A	PO4997
A	HOH1002
A	HOH1009
A	HOH1013
A	HOH1016
A	HOH1043

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NTZ A 998

Chain	Residue
A	LEU136
A	HIS377
A	THR378
A	VAL455
A	ASN484
A	TYR573
A	GLU672
A	ALA673
A	SER674
A	GLY675
A	PO4997
A	HOH1029
A	HOH1043
A	HOH1066

site_id	AC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP B 999

Chain	Residue
B	TYR90
B	TRP491
B	LYS568
B	LYS574
B	TYR648
B	ARG649
B	VAL650
B	GLY675
B	THR676
B	GLY677
B	LYS680
B	PO4997
B	HOH1011
B	HOH1018
B	HOH1022
B	HOH1025
B	HOH1052

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NTZ B 998

Chain	Residue
B	GLY675
B	PO4997
B	HOH1038
B	HOH1052
B	HOH1075
B	LEU136
B	LEU139
B	HIS377
B	THR378
B	ASN484
B	TYR573
B	GLU672
B	ALA673
B	SER674

site_id	AC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP C 999

Chain	Residue
C	TYR90
C	LYS568
C	LYS574
C	TYR648
C	ARG649
C	VAL650
C	GLY675
C	THR676
C	GLY677
C	LYS680
C	PO4997
C	HOH1002
C	HOH1009
C	HOH1013
C	HOH1016
C	HOH1038
C	HOH1044

site_id	BC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NTZ C 998

Chain	Residue
C	LEU136
C	HIS377
C	VAL455
C	ASN484
C	TYR573
C	GLU672
C	ALA673
C	SER674
C	GLY675
C	PO4997
C	HOH1029
C	HOH1044
C	HOH1066

site_id	BC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PLP D 999

Chain	Residue
D	TYR90
D	TRP491
D	LYS568
D	LYS574
D	ARG649
D	VAL650
D	ALA653
D	GLY675
D	THR676
D	GLY677
D	LYS680
D	PO4997
D	HOH1019
D	HOH1023
D	HOH1026
D	HOH1047
D	HOH1053

site_id	BC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NTZ D 998

Chain	Residue
D	LEU136
D	HIS377
D	THR378
D	ASN484
D	TYR573
D	GLU672
D	ALA673
D	SER674
D	GLY675
D	PO4997
D	HOH1039
D	HOH1053
D	HOH1076

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)