1C8L

SYNERGISTIC INHIBITION OF GLYCOGEN PHOSPHORYLASE A BY A POTENTIAL ANTIDIABETIC DRUG AND CAFFEINE

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	18
Details	BINDING SITE FOR RESIDUE PLP A 999

Chain	Residue
A	TYR90
A	THR676
A	GLY677
A	LYS680
A	HOH1024
A	HOH1051
A	HOH1057
A	HOH1108
A	HOH1145
A	HOH1156
A	GLY135
A	TRP491
A	LYS568
A	LYS574
A	TYR648
A	ARG649
A	VAL650
A	GLY675

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE BIN A 930

Chain	Residue
A	VAL40
A	LYS41
A	VAL45
A	GLN71
A	GLN72
A	TYR75
A	ARG193
A	ARG242
A	ARG309
A	ARG310
A	HOH1345
A	HOH1351
A	HOH1532
A	HOH1682

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CFF A 940

Chain	Residue
A	ASN282
A	PHE285
A	HIS571
A	ALA610
A	GLY612
A	TYR613
A	HOH1229
A	HOH1255

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 998

Chain	Residue
A	HIS377
A	ASN484
A	GLU672
A	ALA673
A	SER674
A	GLY675
A	HOH1108
A	HOH1135

---

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	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P11217

Chain	Residue	Details
A	ARG43
A	ARG310

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:3616621

Chain	Residue	Details
A	GLU76

---

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	ASP109
A	PHE143

---

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	GLY156

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N-acetylserine => ECO:0000269|PubMed:3015680

Chain	Residue	Details
A	ARG2

---

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	VAL15

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09812

Chain	Residue	Details
A	GLY204
A	ASP227

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3

Chain	Residue	Details
A	LEU430

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3

Chain	Residue	Details
A	GLU473

---

site_id	SWS_FT_FI10
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09812

Chain	Residue	Details
A	ASP514
A	SER747
A	GLY748

---

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	PHE681

---

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	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

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