Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3S1A

Crystal structure of the phosphorylation-site double mutant S431E/T432E of the KaiC circadian clock protein

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0003677	molecular_function	DNA binding
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0006355	biological_process	regulation of DNA-templated transcription
A	0007623	biological_process	circadian rhythm
A	0009649	biological_process	entrainment of circadian clock
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0042752	biological_process	regulation of circadian rhythm
A	0042754	biological_process	negative regulation of circadian rhythm
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0048511	biological_process	rhythmic process
A	0070297	biological_process	regulation of phosphorelay signal transduction system
A	0106310	molecular_function	protein serine kinase activity
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003677	molecular_function	DNA binding
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0006355	biological_process	regulation of DNA-templated transcription
B	0007623	biological_process	circadian rhythm
B	0009649	biological_process	entrainment of circadian clock
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0042752	biological_process	regulation of circadian rhythm
B	0042754	biological_process	negative regulation of circadian rhythm
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0048511	biological_process	rhythmic process
B	0070297	biological_process	regulation of phosphorelay signal transduction system
B	0106310	molecular_function	protein serine kinase activity
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0003677	molecular_function	DNA binding
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0006355	biological_process	regulation of DNA-templated transcription
C	0007623	biological_process	circadian rhythm
C	0009649	biological_process	entrainment of circadian clock
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0016787	molecular_function	hydrolase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0042752	biological_process	regulation of circadian rhythm
C	0042754	biological_process	negative regulation of circadian rhythm
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0048511	biological_process	rhythmic process
C	0070297	biological_process	regulation of phosphorelay signal transduction system
C	0106310	molecular_function	protein serine kinase activity
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0003677	molecular_function	DNA binding
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0006355	biological_process	regulation of DNA-templated transcription
D	0007623	biological_process	circadian rhythm
D	0009649	biological_process	entrainment of circadian clock
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0016787	molecular_function	hydrolase activity
D	0016887	molecular_function	ATP hydrolysis activity
D	0042752	biological_process	regulation of circadian rhythm
D	0042754	biological_process	negative regulation of circadian rhythm
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0048511	biological_process	rhythmic process
D	0070297	biological_process	regulation of phosphorelay signal transduction system
D	0106310	molecular_function	protein serine kinase activity
E	0000166	molecular_function	nucleotide binding
E	0000287	molecular_function	magnesium ion binding
E	0003677	molecular_function	DNA binding
E	0004674	molecular_function	protein serine/threonine kinase activity
E	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0006355	biological_process	regulation of DNA-templated transcription
E	0007623	biological_process	circadian rhythm
E	0009649	biological_process	entrainment of circadian clock
E	0016301	molecular_function	kinase activity
E	0016740	molecular_function	transferase activity
E	0016787	molecular_function	hydrolase activity
E	0016887	molecular_function	ATP hydrolysis activity
E	0042752	biological_process	regulation of circadian rhythm
E	0042754	biological_process	negative regulation of circadian rhythm
E	0042802	molecular_function	identical protein binding
E	0046872	molecular_function	metal ion binding
E	0048511	biological_process	rhythmic process
E	0070297	biological_process	regulation of phosphorelay signal transduction system
E	0106310	molecular_function	protein serine kinase activity
F	0000166	molecular_function	nucleotide binding
F	0000287	molecular_function	magnesium ion binding
F	0003677	molecular_function	DNA binding
F	0004674	molecular_function	protein serine/threonine kinase activity
F	0004712	molecular_function	protein serine/threonine/tyrosine kinase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0006355	biological_process	regulation of DNA-templated transcription
F	0007623	biological_process	circadian rhythm
F	0009649	biological_process	entrainment of circadian clock
F	0016301	molecular_function	kinase activity
F	0016740	molecular_function	transferase activity
F	0016787	molecular_function	hydrolase activity
F	0016887	molecular_function	ATP hydrolysis activity
F	0042752	biological_process	regulation of circadian rhythm
F	0042754	biological_process	negative regulation of circadian rhythm
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding
F	0048511	biological_process	rhythmic process
F	0070297	biological_process	regulation of phosphorelay signal transduction system
F	0106310	molecular_function	protein serine kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP A 901

Chain	Residue
A	THR290
A	ARG451
A	ILE472
A	HOH527
A	MG801
A	MG802
B	LYS457
B	MET458
B	ARG459
B	GLY460
B	SER461
A	GLY291
B	TRP462
B	HIS463
B	LYS465
A	THR292
A	GLY293
A	LYS294
A	THR295
A	LEU296
A	ASN327
A	TRP331

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP A 903

Chain	Residue
A	GLY49
A	THR50
A	GLY51
A	LYS52
A	THR53
A	LEU54
A	GLU78
A	SER89
A	PHE90
A	ARG218
A	ILE239
A	THR240
A	ASP241
A	MG701
B	LYS224
B	LEU225
B	ARG226
B	THR228
B	SER229
B	HIS230
B	LYS232
B	MG702

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 801

Chain	Residue
A	THR295
A	GLU319
A	ASP378
A	HOH527
A	ATP901
B	ARG459

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 802

Chain	Residue
A	THR290
A	LYS294
A	THR415
A	ATP901
B	GLU432

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 701

Chain	Residue
A	THR53
A	ASP145
A	ATP903

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 526

Chain	Residue
A	GLU431
A	GLU432
A	LYS457
F	THR290
F	ATP901

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 702

Chain	Residue
A	SER48
A	ATP903
B	GLU198
B	PHE199
B	LYS224

site_id	AC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ATP B 901

Chain	Residue
B	THR290
B	GLY291
B	THR292
B	GLY293
B	LYS294
B	THR295
B	LEU296
B	GLU318
B	TRP331
B	ARG451
B	ILE472
B	HOH526
B	HOH527
B	MG801
B	MG802
C	LYS457
C	MET458
C	ARG459
C	SER461
C	HIS463
C	LYS465

site_id	AC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP B 903

Chain	Residue
B	MG701
C	LYS224
C	LEU225
C	ARG226
C	THR228
C	SER229
C	HIS230
C	LYS232
B	GLY49
B	THR50
B	GLY51
B	LYS52
B	THR53
B	LEU54
B	SER89
B	PHE90
B	ILE239
B	ASP241

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG B 801

Chain	Residue
B	THR295
B	GLU318
B	ASP378
B	HOH526
B	HOH527
B	HOH530
B	ATP901

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 802

Chain	Residue
B	THR290
B	LYS294
B	THR415
B	ATP901
C	GLU432

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 701

Chain	Residue
B	LYS52
B	THR53
B	ASP145
B	THR181
B	ATP903

site_id	BC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE ATP C 901

Chain	Residue
C	THR290
C	GLY291
C	THR292
C	GLY293
C	LYS294
C	THR295
C	LEU296
C	GLU318
C	SER330
C	TRP331
C	ARG451
C	ILE472
C	HOH526
C	HOH527
C	MG801
C	MG802
D	LYS457
D	MET458
D	ARG459
D	SER461
D	TRP462
D	HIS463
D	LYS465

site_id	BC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP C 903

Chain	Residue
C	SER48
C	GLY49
C	THR50
C	GLY51
C	LYS52
C	THR53
C	LEU54
C	SER89
C	PHE90
C	ILE239
C	THR240
C	MG701
C	MG702
D	LYS224
D	LEU225
D	ARG226
D	GLY227
D	THR228
D	SER229
D	HIS230

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 802

Chain	Residue
C	THR290
C	THR415
C	ATP901
D	GLU432

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 801

Chain	Residue
C	THR295
C	GLU318
C	GLU319
C	HOH526
C	HOH527
C	ATP901

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 701

Chain	Residue
C	THR53
C	ASP145
C	MG702
C	ATP903

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 702

Chain	Residue
C	THR53
C	GLU78
C	MG701
C	ATP903
D	ARG226

site_id	CC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP D 901

Chain	Residue
D	THR290
D	GLY291
D	THR292
D	GLY293
D	LYS294
D	THR295
D	LEU296
D	GLU318
D	TRP331
D	ARG451
D	ILE472
D	HOH526
D	MG801
D	MG802
E	LYS457
E	MET458
E	ARG459
E	GLY460
E	SER461
E	TRP462
E	HIS463
E	LYS465

site_id	CC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ATP D 903

Chain	Residue
D	GLY49
D	THR50
D	GLY51
D	LYS52
D	THR53
D	LEU54
D	GLU78
D	SER89
D	PHE90
D	ARG218
D	ILE239
D	THR240
D	ASP241
D	HOH529
D	HOH533
D	MG701
D	MG702
E	LYS224
E	LEU225
E	ARG226
E	THR228
E	SER229
E	HIS230
E	LYS232

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 802

Chain	Residue
D	THR295
D	GLU318
D	HOH526
D	HOH527
D	ATP901

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 801

Chain	Residue
D	THR290
D	LYS294
D	THR415
D	ATP901
E	GLU432

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 701

Chain	Residue
D	SER48
D	LYS52
D	ATP903
E	PHE199

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 702

Chain	Residue
D	LYS52
D	THR53
D	HOH528
D	HOH529
D	ATP903

site_id	CC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ATP E 901

Chain	Residue
E	THR290
E	GLY291
E	THR292
E	GLY293
E	LYS294
E	THR295
E	LEU296
E	TRP331
E	ARG451
E	ILE472
E	SER473
E	ASP474
E	MG801
E	MG802
F	LYS457
F	MET458
F	ARG459
F	SER461
F	TRP462
F	HIS463
F	LYS465

site_id	CC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP E 903

Chain	Residue
E	GLY49
E	THR50
E	GLY51
E	LYS52
E	THR53
E	LEU54
E	GLU78
E	SER89
E	PHE90
E	ILE239
E	ASP241
E	HOH533
F	LYS224
F	LEU225
F	ARG226
F	THR228
F	SER229
F	HIS230
F	LYS232
F	HOH537

site_id	CC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG E 801

Chain	Residue
E	THR295
E	GLU318
E	ATP901

site_id	DC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 802

Chain	Residue
E	THR290
E	THR415
E	ATP901
F	GLU432
F	LYS457

site_id	DC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP F 901

Chain	Residue
A	LYS457
A	MET458
A	ARG459
A	SER461
A	HIS463
A	MG526
F	THR290
F	GLY291
F	THR292
F	GLY293
F	LYS294
F	THR295
F	LEU296
F	GLU318
F	TRP331
F	ARG451
F	ILE472
F	ASP474
F	HOH535
F	MG802

site_id	DC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP F 903

Chain	Residue
A	LYS224
A	ARG226
A	THR228
A	SER229
A	HIS230
A	LYS232
F	GLY49
F	THR50
F	GLY51
F	LYS52
F	THR53
F	LEU54
F	GLU78
F	SER89
F	PHE90
F	ILE239
F	THR240
F	ASP241
F	MG701
F	MG702

site_id	DC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG F 701

Chain	Residue
F	THR53
F	ASP145
F	ATP903

site_id	DC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG F 702

Chain	Residue
A	PHE199
A	LYS224
F	SER48
F	GLY49
F	LYS52
F	ATP903

site_id	DC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 802

Chain	Residue
F	THR295
F	GLU318
F	GLU319
F	ATP901

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	42
Details	Region: {"description":"B-loop, required to bind KaiB and SasA","evidences":[{"source":"UniProtKB","id":"Q79V60","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	72
Details	Region: {"description":"Linker","evidences":[{"source":"PubMed","id":"15304218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	54
Details	Region: {"description":"A-loop, interacts with KaiA","evidences":[{"source":"PubMed","id":"18728181","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Active site: {"description":"Proton acceptor in CI (KaiC 1)","evidences":[{"source":"PubMed","id":"22304631","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Active site: {"description":"Proton acceptor in CII (KaiC 2)","evidences":[{"source":"PubMed","id":"22304631","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	150
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01836","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15304218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16628225","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22304631","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TF7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DUG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01836","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"4DUG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TL6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7DXQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01836","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15304218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16628225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TF7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GBL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01836","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15304218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16628225","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1U9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DUG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7DXQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01836","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15304218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16628225","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_01836","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15347809","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15347812","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17717528","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17916691","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1U9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GBL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_01836","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15304218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15347809","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15347812","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17717528","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17916691","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1U9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GBL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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