Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1ZP9

Crystal Structure of full-legnth A.fulgidus Rio1 Serine Kinase bound to ATP and Mn2+ ions.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006338	biological_process	chromatin remodeling
A	0006468	biological_process	protein phosphorylation
A	0016310	biological_process	phosphorylation
A	0016787	molecular_function	hydrolase activity
A	0044024	molecular_function	histone H2AS1 kinase activity
A	0046872	molecular_function	metal ion binding
A	0106310	molecular_function	protein serine kinase activity
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006338	biological_process	chromatin remodeling
B	0006468	biological_process	protein phosphorylation
B	0016310	biological_process	phosphorylation
B	0016787	molecular_function	hydrolase activity
B	0044024	molecular_function	histone H2AS1 kinase activity
B	0046872	molecular_function	metal ion binding
B	0106310	molecular_function	protein serine kinase activity
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0006338	biological_process	chromatin remodeling
C	0006468	biological_process	protein phosphorylation
C	0016310	biological_process	phosphorylation
C	0016787	molecular_function	hydrolase activity
C	0044024	molecular_function	histone H2AS1 kinase activity
C	0046872	molecular_function	metal ion binding
C	0106310	molecular_function	protein serine kinase activity
D	0004672	molecular_function	protein kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005524	molecular_function	ATP binding
D	0006338	biological_process	chromatin remodeling
D	0006468	biological_process	protein phosphorylation
D	0016310	biological_process	phosphorylation
D	0016787	molecular_function	hydrolase activity
D	0044024	molecular_function	histone H2AS1 kinase activity
D	0046872	molecular_function	metal ion binding
D	0106310	molecular_function	protein serine kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 259

Chain	Residue
A	ASN201
A	ASP212
A	ATP260
A	HOH1229
A	HOH1858

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 259

Chain	Residue
B	HOH1805
B	ASN201
B	ASP212
B	ATP260
B	HOH1140

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 259

Chain	Residue
C	ASN201
C	ASP212
C	ATP260
C	HOH1338
C	HOH1784

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 259

Chain	Residue
D	ASN201
D	ASP212
D	ATP260
D	HOH1115
D	HOH1899

site_id	AC5
Number of Residues	29
Details	BINDING SITE FOR RESIDUE ATP A 260

Chain	Residue
A	ILE55
A	SER56
A	ALA61
A	ALA78
A	LYS80
A	TYR82
A	PRO135
A	MSE147
A	GLU148
A	PHE149
A	ILE150
A	THR159
A	ASN201
A	MSE203
A	ILE211
A	ASP212
A	MN259
A	HOH1028
A	HOH1046
A	HOH1081
A	HOH1113
A	HOH1118
A	HOH1229
A	HOH1414
A	HOH1540
A	HOH1741
A	HOH1858
A	HOH1910
B	HOH1068

site_id	AC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ATP B 260

Chain	Residue
A	HOH1075
B	ILE55
B	SER56
B	GLU60
B	ALA78
B	LYS80
B	TYR82
B	PRO135
B	MSE147
B	GLU148
B	PHE149
B	ILE150
B	ASN201
B	ILE211
B	ASP212
B	MN259
B	HOH1025
B	HOH1034
B	HOH1056
B	HOH1101
B	HOH1140
B	HOH1348
B	HOH1499
B	HOH1705
B	HOH1722
B	HOH1805

site_id	AC7
Number of Residues	27
Details	BINDING SITE FOR RESIDUE ATP C 260

Chain	Residue
C	HOH1601
C	HOH1784
D	HOH1376
C	ILE55
C	GLU60
C	ALA61
C	ALA78
C	LYS80
C	TYR82
C	MSE147
C	GLU148
C	PHE149
C	ILE150
C	PRO156
C	THR159
C	ASN201
C	ILE211
C	ASP212
C	MN259
C	HOH1011
C	HOH1013
C	HOH1158
C	HOH1265
C	HOH1312
C	HOH1334
C	HOH1358
C	HOH1410

site_id	AC8
Number of Residues	30
Details	BINDING SITE FOR RESIDUE ATP D 260

Chain	Residue
C	HOH1357
D	ILE55
D	SER56
D	GLU60
D	ALA61
D	ALA78
D	LYS80
D	TYR82
D	PRO135
D	MSE147
D	GLU148
D	PHE149
D	ILE150
D	PRO156
D	THR159
D	ASN201
D	ILE211
D	ASP212
D	MN259
D	HOH1098
D	HOH1166
D	HOH1180
D	HOH1197
D	HOH1200
D	HOH1213
D	HOH1283
D	HOH1303
D	HOH1340
D	HOH1548
D	HOH1614

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-MSE203

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000250\|UniProtKB:Q9BRS2, ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ASP196
B	ASP196
C	ASP196
D	ASP196

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: 4-aspartylphosphate intermediate => ECO:0000250\|UniProtKB:Q9BRS2

Chain	Residue	Details
A	ASP212
B	ASP212
C	ASP212
D	ASP212

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE55
B	ILE55
C	ILE55
D	ILE55

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000269\|PubMed:16008568, ECO:0007744\|PDB:1ZP9

Chain	Residue	Details
A	LYS80
B	LYS80
C	LYS80
D	LYS80

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:16008568, ECO:0007744\|PDB:1ZP9

Chain	Residue	Details
A	GLU148
A	ILE150
B	GLU148
B	ILE150
C	GLU148
C	ILE150
D	GLU148
D	ILE150

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:O30245

Chain	Residue	Details
A	TYR200
B	TYR200
C	TYR200
D	TYR200

site_id	SWS_FT_FI7
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305\|PubMed:16008568

Chain	Residue	Details
A	ASN201
A	ASP212
B	ASN201
B	ASP212
C	ASN201
C	ASP212
D	ASN201
D	ASP212

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269\|PubMed:16008568

Chain	Residue	Details
A	SER108
B	SER108
C	SER108
D	SER108

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)