3RE4

Crystal Structure of Archaeoglobus Fulgidus Rio1 Kinase bound to Toyocamycin.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0106310	molecular_function	protein serine kinase activity
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
B	0106310	molecular_function	protein serine kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE TO1 A 259

Chain	Residue
A	ILE55
A	THR159
A	ILE211
A	ASP212
A	HOH263
A	HOH275
A	HOH279
A	HOH342
A	SER56
A	ALA78
A	PRO135
A	MET147
A	GLU148
A	PHE149
A	ILE150
A	PRO156

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE TO1 B 259

Chain	Residue
B	ILE55
B	SER56
B	ALA78
B	PRO135
B	MET147
B	GLU148
B	PHE149
B	ILE150
B	PRO156
B	ILE211
B	ASP212
B	HOH268
B	HOH279
B	HOH295
B	HOH298

---

Functional Information from PROSITE/UniProt

site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. LVHaDLSEYNIMY

Chain	Residue	Details
A	LEU192-TYR204

---

site_id	PS01245
Number of Residues	12
Details	RIO1 RIO1/ZK632.3/MJ0444 family signature. LVHADLSEYNiM

Chain	Residue	Details
A	LEU192-MET203

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q9BRS2","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"Q9BRS2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16008568","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZP9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16008568","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZP9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O30245","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16008568","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"16008568","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---