1TYY

Crystal structure of aminoimidazole riboside kinase from Salmonella enterica

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0006000	biological_process	fructose metabolic process
A	0008865	molecular_function	fructokinase activity
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0046835	biological_process	carbohydrate phosphorylation
A	0046872	molecular_function	metal ion binding
B	0005524	molecular_function	ATP binding
B	0006000	biological_process	fructose metabolic process
B	0008865	molecular_function	fructokinase activity
B	0016301	molecular_function	kinase activity
B	0016310	biological_process	phosphorylation
B	0046835	biological_process	carbohydrate phosphorylation
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K A 404

Chain	Residue
A	ASP246
A	THR248
A	ALA287
A	GLY292

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K A 405

Chain	Residue
A	ALA180
A	ALA181
A	ALA183
A	GLY213

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE K B 504

Chain	Residue
B	ALA181
B	ALA183
B	GLY213
B	ALA180

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE K B 505

Chain	Residue
B	ASP246
B	THR248
B	ALA287

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Functional Information from PROSITE/UniProt

site_id	PS00584
Number of Residues	14
Details	PFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. DTtGAGDafvGGLL

Chain	Residue	Details
A	ASP246-LEU259

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:15458630, ECO:0007744|PDB:1TZ3

Chain	Residue	Details
A	ASP252
B	ASP252

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site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:15458630, ECO:0007744|PDB:1TZ3, ECO:0007744|PDB:1TZ6

Chain	Residue	Details
A	ASP16
B	ASP252
B	ALA290
B	GLY292
A	GLY31
A	ARG162
A	ASP252
A	ALA290
A	GLY292
B	ASP16
B	GLY31
B	ARG162

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:15458630, ECO:0007744|PDB:1TZ6

Chain	Residue	Details
A	TYR101
B	TYR101

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	BINDING: BINDING => ECO:0000305|PubMed:15458630, ECO:0007744|PDB:1TZ6

Chain	Residue	Details
A	ASP158
B	ASN281
A	LYS187
A	GLU192
A	SER220
A	ASN281
B	ASP158
B	LYS187
B	GLU192
B	SER220

---

site_id	SWS_FT_FI5
Number of Residues	14
Details	BINDING: BINDING => ECO:0000269|PubMed:15458630, ECO:0007744|PDB:1TYY, ECO:0007744|PDB:1TZ3, ECO:0007744|PDB:1TZ6

Chain	Residue	Details
A	ALA180
B	ALA183
B	GLY213
B	ASP246
B	THR248
B	ALA287
A	ALA181
A	ALA183
A	GLY213
A	ASP246
A	THR248
A	ALA287
B	ALA180
B	ALA181

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1lio

Chain	Residue	Details
A	ASP252

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site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1lio

Chain	Residue	Details
B	ASP252

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site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1lio

Chain	Residue	Details
A	GLY249
A	GLY251
A	ASP252
A	ALA250

---

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1lio

Chain	Residue	Details
B	GLY249
B	GLY251
B	ASP252
B	ALA250

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 751

Chain	Residue	Details
A	GLY249	electrostatic stabiliser
A	ALA250	electrostatic stabiliser
A	GLY251	electrostatic stabiliser
A	ASP252	electrostatic stabiliser, proton shuttle (general acid/base)

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 751

Chain	Residue	Details
B	GLY249	electrostatic stabiliser
B	ALA250	electrostatic stabiliser
B	GLY251	electrostatic stabiliser
B	ASP252	electrostatic stabiliser, proton shuttle (general acid/base)

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