2PYI

Crystal structure of Glycogen Phosphorylase in complex with glucosyl triazoleacetamide

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	20
Details	BINDING SITE FOR RESIDUE DL8 A 998

Chain	Residue
A	LEU136
A	ASN484
A	TYR573
A	GLU672
A	ALA673
A	SER674
A	GLY675
A	HOH1042
A	HOH1166
A	HOH1266
A	HOH1413
A	ASN282
A	HOH1685
A	ASP283
A	ASN284
A	PHE286
A	ASP339
A	HIS341
A	HIS377
A	ALA383

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS A 931

Chain	Residue
A	TRP67
A	ILE68
A	ARG193

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMS A 936

Chain	Residue
A	GLN219
A	LYS294

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS A 937

Chain	Residue
A	HIS201
A	TRP215
A	ARG351
A	LEU356
A	HOH1067

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMS A 938

Chain	Residue
A	ARG519
A	GLU701
A	GLU702
A	ALA703
A	GLY704
A	HOH1153

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS A 939

Chain	Residue
A	GLU706
A	PHE708
A	PHE709
A	ARG786
A	HOH1743

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMS A 940

Chain	Residue
A	ARG66
A	LEU102
A	ARG234
A	ASN236
A	ARG833
A	HOH1104

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMS A 942

Chain	Residue
A	TYR548
A	GLU552
A	TYR553
A	ARG649
A	HOH1321
A	HOH1700

---

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMS A 945

Chain	Residue
A	GLN264
A	LEU267
A	ASP268
A	ASN270
A	LEU271
A	ASN274

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS A 946

Chain	Residue
A	TYR553
A	PHE644
A	LEU645
A	GLU646
A	HOH1120

---

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS A 972

Chain	Residue
A	LEU271
A	ASN274
A	HOH1605

---

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	ASP42
A	ARG309

---

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

Chain	Residue	Details
A	TYR75

---

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	CYS108
A	CYS142

---

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	TYR155

---

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

Chain	Residue	Details
A	SER1

---

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	SER14

---

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

Chain	Residue	Details
A	TYR203
A	TYR226

---

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

Chain	Residue	Details
A	SER429

---

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

Chain	Residue	Details
A	TYR472

---

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

Chain	Residue	Details
A	SER513
A	SER746
A	SER747

---

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	LLP680

---

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	HIS377	electrostatic stabiliser
A	LYS568	electrostatic stabiliser
A	ARG569	electrostatic stabiliser
A	LYS574	electrostatic stabiliser
A	THR676	electrostatic stabiliser
A	LLP680	covalently attached

---