1AXR

COOPERATIVITY BETWEEN HYDROGEN-BONDING AND CHARGE-DIPOLE INTERACTIONS IN THE INHIBITION OF BETA-GLYCOSIDASES BY AZOLOPYRIDINES: EVIDENCE FROM A STUDY WITH GLYCOGEN PHOSPHORYLASE B

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	3
Details	BINDING SITE FOR RESIDUE PO4 A 996

Chain	Residue
A	TYR75
A	ARG309
A	ARG310

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site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 997

Chain	Residue
A	PLP999
A	HOH1194
A	HOH1412
A	GLY135
A	ARG569
A	TYR573
A	LYS574
A	GLU672
A	HTP998

---

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PLP A 999

Chain	Residue
A	TYR90
A	GLY135
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	HOH1229
A	HOH1298
A	HOH1299
A	HOH1305
A	HOH1412

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HTP A 998

Chain	Residue
A	GLY135
A	LEU136
A	LEU139
A	ASN284
A	HIS377
A	VAL455
A	ASN484
A	TYR573
A	GLU672
A	SER674
A	GLY675
A	PO4997
A	HOH1273
A	HOH1370
A	HOH1412

---

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	HIS377	electrostatic stabiliser
A	LYS568	electrostatic stabiliser
A	ARG569	electrostatic stabiliser
A	LYS574	electrostatic stabiliser
A	THR676	electrostatic stabiliser
A	LYS680	covalently attached

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