Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1U9I

Crystal Structure of Circadian Clock Protein KaiC with Phosphorylation Sites

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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	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	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	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	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	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	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	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	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	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	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	4
Details	BINDING SITE FOR RESIDUE MG A 520

Chain	Residue
A	THR295
A	GLU318
A	GLU319
A	ATP521

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 520

Chain	Residue
B	THR295
B	GLU318
B	ASP378
B	ATP521

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 520

Chain	Residue
C	GLU318
C	GLU319
C	ATP521
C	THR295

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 520

Chain	Residue
D	THR295
D	GLU318
D	ATP521

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 520

Chain	Residue
E	THR295
E	GLU318
E	GLU319
E	ASP378
E	ATP601

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 520

Chain	Residue
F	THR295
F	GLU318
F	GLU319
F	ATP701
F	HOH726

site_id	AC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP A 521

Chain	Residue
A	THR290
A	GLY291
A	THR292
A	GLY293
A	LYS294
A	THR295
A	LEU296
A	TRP331
A	ARG451
A	ILE472
A	MG520
B	LYS457
B	MET458
B	ARG459
B	GLY460
B	SER461
B	TRP462
B	HIS463
B	LYS465

site_id	AC8
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP A 522

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

site_id	AC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP B 521

Chain	Residue
B	THR290
B	GLY291
B	THR292
B	GLY293
B	LYS294
B	THR295
B	LEU296
B	TRP331
B	ARG451
B	ILE472
B	MG520
C	LYS457
C	MET458
C	ARG459
C	SER461
C	TRP462
C	HIS463
C	LYS465

site_id	BC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ATP B 522

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

site_id	BC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP C 521

Chain	Residue
C	THR292
C	GLY293
C	LYS294
C	THR295
C	LEU296
C	SER330
C	TRP331
C	ARG451
C	ILE472
C	MG520
D	LYS457
D	MET458
D	ARG459
D	SER461
D	TRP462
D	HIS463
D	LYS465
D	HOH528
C	THR290
C	GLY291

site_id	BC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ATP C 522

Chain	Residue
C	GLY49
C	THR50
C	GLY51
C	LYS52
C	THR53
C	LEU54
C	SER89
C	PHE90
C	ILE239
C	THR240
C	ASP241
D	LYS224
D	ARG226
D	THR228
D	HIS230
D	LYS232

site_id	BC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ATP D 521

Chain	Residue
D	THR290
D	GLY291
D	THR292
D	GLY293
D	LYS294
D	THR295
D	LEU296
D	SER330
D	TRP331
D	ARG451
D	ILE472
D	ASP474
D	MG520
E	LYS457
E	MET458
E	ARG459
E	SER461
E	TRP462
E	HIS463
E	LYS465

site_id	BC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP D 522

Chain	Residue
D	GLY49
D	THR50
D	GLY51
D	LYS52
D	THR53
D	LEU54
D	GLU78
D	SER89
D	PHE90
D	ILE239
D	THR240
D	ASP241
E	LYS224
E	ARG226
E	THR228
E	SER229
E	HIS230
E	HOH613

site_id	BC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP E 601

Chain	Residue
E	THR290
E	GLY291
E	THR292
E	GLY293
E	LYS294
E	THR295
E	LEU296
E	TRP331
E	ARG451
E	ILE472
E	ASP474
E	MG520
F	LYS457
F	MET458
F	ARG459
F	SER461
F	TRP462
F	HIS463
F	LYS465

site_id	BC7
Number of Residues	17
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	ILE239
E	ASP241
F	LYS224
F	ARG226
F	THR228
F	SER229
F	HIS230
F	LYS232

site_id	BC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP F 701

Chain	Residue
A	LYS457
A	MET458
A	ARG459
A	SER461
A	TRP462
A	HIS463
A	LYS465
F	THR290
F	GLY291
F	THR292
F	GLY293
F	LYS294
F	THR295
F	LEU296
F	SER330
F	TRP331
F	ARG451
F	ILE472
F	SER473
F	ASP474
F	MG520
F	HOH726

site_id	BC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ATP F 703

Chain	Residue
A	LYS224
A	ARG226
A	THR228
A	HIS230
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	HOH716

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor in CI (KaiC 1) => ECO:0000305\|PubMed:22304631

Chain	Residue	Details
C	GLU77
D	GLU77
E	GLU77
F	GLU77

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor in CII (KaiC 2) => ECO:0000305\|PubMed:22304631

Chain	Residue	Details
C	GLU318
D	GLU318
E	GLU318
F	GLU318

site_id	SWS_FT_FI3
Number of Residues	50
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01836, ECO:0000269\|PubMed:15304218, ECO:0000269\|PubMed:16628225, ECO:0000269\|PubMed:22304631, ECO:0007744\|PDB:1TF7, ECO:0007744\|PDB:2GBL, ECO:0007744\|PDB:4DUG

Chain	Residue	Details
C	GLY49
C	HIS230
F	LYS465
C	THR240
C	ASP241
C	THR290
C	GLY291
C	THR292
C	GLY293
C	LYS294
C	LEU296
C	TRP331
C	THR50
C	ARG451
C	LYS457
C	ARG459
C	SER461
C	HIS463
C	LYS465
D	GLY49
D	THR50
D	GLY51
D	LYS52
C	GLY51
D	LEU54
D	SER89
D	LYS224
D	ARG226
D	THR228
D	HIS230
D	THR240
D	ASP241
D	THR290
D	GLY291
C	LYS52
D	THR292
D	GLY293
D	LYS294
D	LEU296
D	TRP331
D	ARG451
D	LYS457
D	ARG459
D	SER461
D	HIS463
C	LEU54
D	LYS465
E	GLY49
E	THR50
E	GLY51
E	LYS52
E	LEU54
E	SER89
E	LYS224
E	ARG226
E	THR228
C	SER89
E	HIS230
E	THR240
E	ASP241
E	THR290
E	GLY291
E	THR292
E	GLY293
E	LYS294
E	LEU296
E	TRP331
C	LYS224
E	ARG451
E	LYS457
E	ARG459
E	SER461
E	HIS463
E	LYS465
F	GLY49
F	THR50
F	GLY51
F	LYS52
C	ARG226
F	LEU54
F	SER89
F	LYS224
F	ARG226
F	THR228
F	HIS230
F	THR240
F	ASP241
F	THR290
F	GLY291
C	THR228
F	THR292
F	GLY293
F	LYS294
F	LEU296
F	TRP331
F	ARG451
F	LYS457
F	ARG459
F	SER461
F	HIS463

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01836, ECO:0007744\|PDB:4DUG, ECO:0007744\|PDB:4TL6, ECO:0007744\|PDB:7DXQ

Chain	Residue	Details
C	THR53
D	THR53
E	THR53
F	THR53

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01836, ECO:0000269\|PubMed:15304218, ECO:0000269\|PubMed:16628225, ECO:0007744\|PDB:1TF7, ECO:0007744\|PDB:2GBL

Chain	Residue	Details
C	LEU225
C	MET458
D	LEU225
D	MET458
E	LEU225
E	MET458
F	LEU225
F	MET458

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01836, ECO:0000269\|PubMed:15304218, ECO:0000269\|PubMed:16628225, ECO:0007744\|PDB:1U9I, ECO:0007744\|PDB:2GBL, ECO:0007744\|PDB:4DUG, ECO:0007744\|PDB:7DXQ

Chain	Residue	Details
C	THR295
D	THR295
E	THR295
F	THR295

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01836, ECO:0000269\|PubMed:15304218, ECO:0000269\|PubMed:16628225

Chain	Residue	Details
C	GLU318
D	GLU318
E	GLU318
F	GLU318

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000255\|HAMAP-Rule:MF_01836, ECO:0000269\|PubMed:15347809, ECO:0000269\|PubMed:15347812, ECO:0000269\|PubMed:17717528, ECO:0000269\|PubMed:17916691, ECO:0007744\|PDB:1U9I, ECO:0007744\|PDB:2GBL

Chain	Residue	Details
C	SER431
D	SER431
E	SEP431
F	SEP431

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000255\|HAMAP-Rule:MF_01836, ECO:0000269\|PubMed:15304218, ECO:0000269\|PubMed:15347809, ECO:0000269\|PubMed:15347812, ECO:0000269\|PubMed:17717528, ECO:0000269\|PubMed:17916691, ECO:0007744\|PDB:1U9I, ECO:0007744\|PDB:2GBL

Chain	Residue	Details
C	TPO432
D	TPO432
E	TPO432
F	TPO432

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