Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4IJM

Crystal structure of circadian clock protein KaiC A422V mutant

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	6
Details	BINDING SITE FOR RESIDUE MG A 801

Chain	Residue
A	THR295
A	GLU319
A	ATP802
A	HOH902
A	HOH950
B	MG606

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP A 802

Chain	Residue
A	GLY293
A	LYS294
A	THR295
A	LEU296
A	GLU318
A	TRP331
A	ARG451
A	ILE472
A	MG801
A	HOH902
B	LYS457
B	MET458
B	ARG459
B	GLY460
B	SER461
B	TRP462
B	HIS463
B	LYS465
B	MG606
A	THR290
A	GLY291
A	THR292

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP A 803

Chain	Residue
A	GLY49
A	THR50
A	GLY51
A	LYS52
A	THR53
A	LEU54
A	SER89
A	PHE90
A	ARG218
A	ILE239
A	THR240
A	ASP241
A	HOH915
A	HOH948
B	LYS224
B	ARG226
B	THR228
B	SER229
B	HIS230
B	HOH729

site_id	AC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP A 804

Chain	Residue
A	LEU223
A	LYS224
A	ARG226
A	THR228
A	SER229
A	HIS230
A	LYS232
A	HOH905
F	GLY49
F	THR50
F	GLY51
F	LYS52
F	THR53
F	LEU54
F	SER89
F	PHE90
F	ILE239
F	THR240
F	ASP241
F	HOH715

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 601

Chain	Residue
B	THR295
B	GLU318
B	ATP602
B	HOH720

site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP B 602

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	MG601
B	HOH720
C	LYS457
C	MET458
C	ARG459
C	SER461
C	TRP462
C	HIS463
C	LYS465

site_id	AC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP B 603

Chain	Residue
B	PHE90
B	ILE239
B	THR240
B	ASP241
B	HOH704
C	LEU223
C	LYS224
C	LEU225
C	ARG226
C	THR228
C	SER229
C	HIS230
B	GLY49
B	THR50
B	GLY51
B	LYS52
B	THR53
B	LEU54
B	SER89

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 604

Chain	Residue
A	ASP155
A	TYR194
B	SER157
B	SER158

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 605

Chain	Residue
B	THR47
B	GLU187
B	ARG216
B	HOH738
C	ILE191

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 606

Chain	Residue
A	MG801
A	ATP802
B	ARG459

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 601

Chain	Residue
C	THR295
C	GLU318
C	GLU319
C	ASP378
C	ATP602

site_id	BC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ATP C 602

Chain	Residue
C	THR290
C	GLY291
C	GLY293
C	LYS294
C	THR295
C	LEU296
C	GLU318
C	TRP331
C	ARG451
C	ILE472
C	ASP474
C	MG601
C	HOH740
D	TPO432
D	LYS457
D	MET458
D	ARG459
D	SER461
D	TRP462
D	HIS463
D	LYS465

site_id	BC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP C 603

Chain	Residue
C	GLY49
C	THR50
C	GLY51
C	LYS52
C	THR53
C	LEU54
C	SER89
C	PHE90
C	ILE239
C	THR240
C	ASP241
C	HOH766
C	HOH769
D	PHE199
D	LEU223
D	LYS224
D	ARG226
D	THR228
D	SER229
D	HIS230

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 C 604

Chain	Residue
C	GLU187
C	ASN209
C	ARG216
D	ILE191

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 601

Chain	Residue
D	THR295
D	GLU319
D	ATP602
D	HOH739

site_id	BC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP D 602

Chain	Residue
D	THR290
D	GLY291
D	GLY293
D	LYS294
D	THR295
D	LEU296
D	GLU318
D	TRP331
D	ARG451
D	ILE472
D	MG601
D	HOH739
E	LYS457
E	MET458
E	ARG459
E	SER461
E	TRP462
E	HIS463
E	LYS465

site_id	BC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP D 603

Chain	Residue
D	GLY49
D	THR50
D	GLY51
D	LYS52
D	THR53
D	LEU54
D	GLU78
D	SER89
D	PHE90
D	ILE239
D	ASP241
D	HOH703
D	HOH716
D	HOH729
E	LEU223
E	LYS224
E	LEU225
E	ARG226
E	THR228
E	SER229
E	HIS230
E	LYS232

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 604

Chain	Residue
D	THR47
D	GLU187
D	ARG216
E	ILE191

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 601

Chain	Residue
E	THR295
E	GLU318
E	ATP602
E	HOH725

site_id	CC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP E 602

Chain	Residue
E	THR290
E	GLY291
E	THR292
E	GLY293
E	LYS294
E	THR295
E	LEU296
E	GLU318
E	TRP331
E	ARG451
E	ILE472
E	MG601
F	LYS457
F	MET458
F	ARG459
F	SER461
F	TRP462
F	HIS463
F	LYS465
F	HOH708

site_id	CC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP E 603

Chain	Residue
E	GLY49
E	THR50
E	GLY51
E	LYS52
E	THR53
E	LEU54
E	GLU78
E	SER89
E	PHE90
E	ARG218
E	ILE239
E	ASP241
E	HOH715
F	LEU223
F	LYS224
F	ARG226
F	THR228
F	SER229
F	HIS230
F	LYS232

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 E 604

Chain	Residue
E	PHE151
E	GLN152
E	TYR154
E	ASP155
F	SER157
F	SER158

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 E 605

Chain	Residue
E	GLU187
E	ARG216
E	HOH712
F	GLY189
F	ILE191

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 601

Chain	Residue
F	THR295
F	GLU318
F	GLU319
F	ASP378
F	ATP602

site_id	CC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ATP F 602

Chain	Residue
A	LYS457
A	MET458
A	ARG459
A	SER461
A	TRP462
A	HIS463
A	LYS465
F	THR290
F	GLY291
F	GLY293
F	LYS294
F	THR295
F	LEU296
F	GLU318
F	SER330
F	TRP331
F	ARG451
F	ILE472
F	SER473
F	ASP474
F	MG601

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 F 603

Chain	Residue
A	ILE191
A	LEU223
F	THR47
F	GLU187
F	ARG216

site_id	CC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 F 604

Chain	Residue
A	LYS232
F	ARG218
F	THR238
F	ILE239

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	45
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)