Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4O0M

Crystal structure of T. Elongatus BP-1 Clock Protein KaiC

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	0006351	biological_process	DNA-templated transcription
A	0006355	biological_process	regulation of DNA-templated transcription
A	0007623	biological_process	circadian rhythm
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	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0048511	biological_process	rhythmic process
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	0006351	biological_process	DNA-templated transcription
B	0006355	biological_process	regulation of DNA-templated transcription
B	0007623	biological_process	circadian rhythm
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	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0048511	biological_process	rhythmic process
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	0006351	biological_process	DNA-templated transcription
C	0006355	biological_process	regulation of DNA-templated transcription
C	0007623	biological_process	circadian rhythm
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	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0048511	biological_process	rhythmic process
C	0106310	molecular_function	protein serine kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 801

Chain	Residue
A	THR295
A	GLU319
A	ATP802

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP A 802

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

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ATP A 803

Chain	Residue
A	GLY50
A	THR51
A	GLY52
A	LYS53
A	THR54
A	LEU55
A	SER90
A	PHE91
A	ILE240
A	MG804
B	LYS225
B	LEU226
B	ARG227
B	THR229
B	THR230
B	HIS231
B	LYS233

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 804

Chain	Residue
A	THR54
A	GLU79
A	ASP146
A	ATP803

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

Chain	Residue
B	THR295
B	GLU318
B	GLU319
B	ATP602

site_id	AC6
Number of Residues	19
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	THR415
B	ARG451
B	ILE472
B	MG601
C	LYS457
C	MET458
C	ARG459
C	SER461
C	TRP462
C	HIS463

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 603

Chain	Residue
B	THR54
B	GLU79
B	ATP604

site_id	AC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP B 604

Chain	Residue
B	SER49
B	GLY50
B	THR51
B	GLY52
B	LYS53
B	THR54
B	LEU55
B	SER90
B	PHE91
B	ARG219
B	ILE240
B	MG603
C	PHE200
C	LYS225
C	LEU226
C	ARG227
C	THR229
C	THR230
C	HIS231

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG C 601

Chain	Residue
C	THR295
C	ATP602

site_id	BC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP C 602

Chain	Residue
C	THR295
C	LEU296
C	TRP331
C	THR415
C	ARG451
C	ILE472
C	MG601
C	HOH704
A	LYS457
A	MET458
A	ARG459
A	SER461
A	HIS463
C	THR290
C	GLY291
C	THR292
C	GLY293
C	LYS294

site_id	BC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP C 603

Chain	Residue
A	PHE200
A	LYS225
A	ARG227
A	THR229
A	THR230
A	HIS231
A	HOH950
C	SER49
C	GLY50
C	THR51
C	GLY52
C	LYS53
C	THR54
C	LEU55
C	SER90
C	PHE91
C	ARG219
C	ILE240
C	MG604

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 604

Chain	Residue
C	THR54
C	ASP146
C	ATP603

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	21
Details	Region: {"description":"B-loop, required to bind KaiB and SasA","evidences":[{"source":"PubMed","id":"24112939","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34618577","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	36
Details	Region: {"description":"Linker","evidences":[{"source":"PubMed","id":"35507871","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	3
Details	Active site: {"description":"Proton acceptor in CI (KaiC 1)","evidences":[{"source":"PubMed","id":"35507871","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	3
Details	Active site: {"description":"Proton acceptor in CII (KaiC 2)","evidences":[{"source":"PubMed","id":"35507871","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PDB","id":"7DY1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	63
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01836","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"7DY1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	21
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01836","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_01836","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24112939","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"HAMAP-Rule","id":"MF_01836","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24112939","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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