Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7DYJ

Crystal Structure of Cyanobacterial Circadian Clock Protein KaiC

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003677	molecular_function	DNA binding
A	0003689	molecular_function	DNA clamp loader activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004676	molecular_function	3-phosphoinositide-dependent protein kinase activity
A	0004677	molecular_function	DNA-dependent protein kinase activity
A	0004679	molecular_function	AMP-activated protein kinase activity
A	0004711	molecular_function	ribosomal protein S6 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	0006338	biological_process	chromatin remodeling
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	0035175	molecular_function	histone H3S10 kinase activity
A	0035402	molecular_function	histone H3T11 kinase activity
A	0035403	molecular_function	histone H3T6 kinase activity
A	0035979	molecular_function	histone H2AXS139 kinase 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	0044022	molecular_function	histone H3S28 kinase activity
A	0044023	molecular_function	histone H4S1 kinase activity
A	0044024	molecular_function	histone H2AS1 kinase activity
A	0044025	molecular_function	histone H2BS14 kinase activity
A	0046872	molecular_function	metal ion binding
A	0048511	biological_process	rhythmic process
A	0061775	molecular_function	cohesin loader activity
A	0070297	biological_process	regulation of phosphorelay signal transduction system
A	0072354	molecular_function	histone H3T3 kinase activity
A	0072371	molecular_function	histone H2AS121 kinase activity
A	0072518	molecular_function	Rho-dependent protein serine/threonine kinase activity
A	0106310	molecular_function	protein serine kinase activity
A	0140584	molecular_function	chromatin extrusion motor activity
A	0140588	biological_process	chromatin looping
A	0140665	molecular_function	ATP-dependent H3-H4 histone complex chaperone activity
A	0140823	molecular_function	histone H2BS36 kinase activity
A	0140849	molecular_function	ATP-dependent H2AZ histone chaperone activity
A	0140855	molecular_function	histone H3S57 kinase activity
A	0140857	molecular_function	histone H3T45 kinase activity
A	1990244	molecular_function	histone H2AT120 kinase activity
B	0000287	molecular_function	magnesium ion binding
B	0003677	molecular_function	DNA binding
B	0003689	molecular_function	DNA clamp loader activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0004676	molecular_function	3-phosphoinositide-dependent protein kinase activity
B	0004677	molecular_function	DNA-dependent protein kinase activity
B	0004679	molecular_function	AMP-activated protein kinase activity
B	0004711	molecular_function	ribosomal protein S6 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	0006338	biological_process	chromatin remodeling
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	0035175	molecular_function	histone H3S10 kinase activity
B	0035402	molecular_function	histone H3T11 kinase activity
B	0035403	molecular_function	histone H3T6 kinase activity
B	0035979	molecular_function	histone H2AXS139 kinase 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	0044022	molecular_function	histone H3S28 kinase activity
B	0044023	molecular_function	histone H4S1 kinase activity
B	0044024	molecular_function	histone H2AS1 kinase activity
B	0044025	molecular_function	histone H2BS14 kinase activity
B	0046872	molecular_function	metal ion binding
B	0048511	biological_process	rhythmic process
B	0061775	molecular_function	cohesin loader activity
B	0070297	biological_process	regulation of phosphorelay signal transduction system
B	0072354	molecular_function	histone H3T3 kinase activity
B	0072371	molecular_function	histone H2AS121 kinase activity
B	0072518	molecular_function	Rho-dependent protein serine/threonine kinase activity
B	0106310	molecular_function	protein serine kinase activity
B	0140584	molecular_function	chromatin extrusion motor activity
B	0140588	biological_process	chromatin looping
B	0140665	molecular_function	ATP-dependent H3-H4 histone complex chaperone activity
B	0140823	molecular_function	histone H2BS36 kinase activity
B	0140849	molecular_function	ATP-dependent H2AZ histone chaperone activity
B	0140855	molecular_function	histone H3S57 kinase activity
B	0140857	molecular_function	histone H3T45 kinase activity
B	1990244	molecular_function	histone H2AT120 kinase activity

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
A	GLU77
B	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
A	GLU318
B	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
A	GLY49
A	HIS230
A	THR240
A	ASP241
A	THR290
A	GLY291
A	THR292
A	GLY293
A	LYS294
A	LEU296
A	TRP331
A	THR50
A	ARG451
A	LYS457
A	ARG459
A	SER461
A	HIS463
A	LYS465
B	GLY49
B	THR50
B	GLY51
B	LYS52
A	GLY51
B	LEU54
B	SER89
B	LYS224
B	ARG226
B	THR228
B	HIS230
B	THR240
B	ASP241
B	THR290
B	GLY291
A	LYS52
B	THR292
B	GLY293
B	LYS294
B	LEU296
B	TRP331
B	ARG451
B	LYS457
B	ARG459
B	SER461
B	HIS463
A	LEU54
B	LYS465
A	SER89
A	LYS224
A	ARG226
A	THR228

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
A	THR53
B	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
A	LEU225
A	MET458
B	LEU225
B	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
A	THR295
B	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
A	GLU318
B	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
A	SER431
B	SER431

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
A	THR432
B	THR432

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