Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1ZTH

Crystal Structure of A.fulgidus Rio1 serine protein kinase bound to ADP and Manganese ion

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
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
C	0106310	molecular_function	protein serine kinase activity
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0004672	molecular_function	protein kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0016787	molecular_function	hydrolase 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 902

Chain	Residue
A	ASN201
A	ASP212
A	ADP901
A	HOH942
A	HOH1073

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 904

Chain	Residue
B	HOH1090
B	ASN201
B	ASP212
B	ADP903
B	HOH911

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 906

Chain	Residue
C	ASN201
C	ASP212
C	ADP905
C	HOH1063

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 908

Chain	Residue
D	ASN201
D	ASP212
D	ADP907
D	HOH948
D	HOH1049

site_id	AC5
Number of Residues	27
Details	BINDING SITE FOR RESIDUE ADP A 901

Chain	Residue
A	ILE55
A	SER56
A	VAL63
A	ALA78
A	LYS80
A	PRO135
A	MSE147
A	GLU148
A	PHE149
A	ILE150
A	PRO156
A	ASN201
A	MSE203
A	ILE211
A	ASP212
A	MN902
A	HOH905
A	HOH912
A	HOH915
A	HOH926
A	HOH942
A	HOH955
A	HOH971
A	HOH990
A	HOH1016
A	HOH1073
B	HOH1108

site_id	AC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ADP B 903

Chain	Residue
A	HOH961
B	ILE55
B	SER56
B	VAL63
B	ALA78
B	LYS80
B	PRO135
B	MSE147
B	GLU148
B	PHE149
B	ILE150
B	ASN201
B	ILE211
B	ASP212
B	MN904
B	HOH905
B	HOH910
B	HOH911
B	HOH918
B	HOH922
B	HOH988
B	HOH1008
B	HOH1009
B	HOH1017
B	HOH1073
B	HOH1090

site_id	AC7
Number of Residues	28
Details	BINDING SITE FOR RESIDUE ADP C 905

Chain	Residue
D	HOH979
C	ILE55
C	SER56
C	ALA78
C	LYS80
C	PRO135
C	MSE147
C	GLU148
C	PHE149
C	ILE150
C	PRO156
C	THR159
C	ASN201
C	ILE211
C	ASP212
C	MN906
C	HOH908
C	HOH910
C	HOH912
C	HOH919
C	HOH924
C	HOH928
C	HOH960
C	HOH974
C	HOH1013
C	HOH1028
C	HOH1046
C	HOH1063

site_id	AC8
Number of Residues	28
Details	BINDING SITE FOR RESIDUE ADP D 907

Chain	Residue
C	HOH1085
D	ILE55
D	SER56
D	VAL63
D	ALA78
D	LYS80
D	PRO135
D	MSE147
D	GLU148
D	PHE149
D	ILE150
D	PRO156
D	THR159
D	ASN201
D	ILE211
D	ASP212
D	MN908
D	HOH914
D	HOH915
D	HOH924
D	HOH935
D	HOH943
D	HOH959
D	HOH983
D	HOH986
D	HOH1019
D	HOH1029
D	HOH1049

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	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	4
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	32
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
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	8
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	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O30245","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16008568","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"16008568","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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