1ZAO

Crystal Structure of A.fulgidus Rio2 Kinase Complexed With ATP and Manganese Ions

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	0005829	cellular_component	cytosol
A	0006468	biological_process	protein phosphorylation
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0030490	biological_process	maturation of SSU-rRNA
A	0030688	cellular_component	preribosome, small subunit precursor
A	0046872	molecular_function	metal ion binding
A	0106310	molecular_function	protein serine kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 283

Chain	Residue
A	ASN223
A	ASP235
A	MN284
A	PO4285
A	ATP286
A	HOH615

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 284

Chain	Residue
A	PO4285
A	ATP286
A	HOH315
A	GLU103
A	ASP235
A	MN283

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 285

Chain	Residue
A	GLU103
A	ASP218
A	ASN223
A	ASP235
A	MN283
A	MN284
A	ATP286
A	HOH309

---

site_id	AC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ATP A 286

Chain	Residue
A	GLU103
A	SER104
A	VAL106
A	VAL118
A	LYS120
A	HIS122
A	HIS126
A	MET179
A	GLU180
A	ILE182
A	GLU186
A	ASN223
A	ILE234
A	ASP235
A	PRO237
A	MN283
A	MN284
A	PO4285
A	HOH294
A	HOH303
A	HOH337
A	HOH350
A	HOH529
A	HOH586

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 287

Chain	Residue
A	GLN162
A	GLY163
A	LEU164
A	VAL166
A	LYS168

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE214-VAL226

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ASP218

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	MET98

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:15943813

Chain	Residue	Details
A	GLU103
A	ASN223
A	ASP235

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305|PubMed:15341724

Chain	Residue	Details
A	LYS120

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:15943813, ECO:0007744|PDB:1ZAO

Chain	Residue	Details
A	HIS126

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:15341724, ECO:0000269|PubMed:15943813, ECO:0007744|PDB:1TQP, ECO:0007744|PDB:1ZAO

Chain	Residue	Details
A	GLU180

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:15341724, ECO:0007744|PDB:1TQP

Chain	Residue	Details
A	TYR222

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:15943813

Chain	Residue	Details
A	SER128

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 2phk

Chain	Residue	Details
A	ASP218
A	SER220

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