5JWQ

Crystal structure of KaiC S431E in complex with foldswitch-stabilized KaiB from Thermosynechococcus elongatus

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	0005515	molecular_function	protein binding
B	0007623	biological_process	circadian rhythm
B	0042326	biological_process	negative regulation of phosphorylation
B	0042802	molecular_function	identical protein binding
B	0048511	biological_process	rhythmic process
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
D	0005515	molecular_function	protein binding
D	0007623	biological_process	circadian rhythm
D	0042326	biological_process	negative regulation of phosphorylation
D	0042802	molecular_function	identical protein binding
D	0048511	biological_process	rhythmic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue ADP A 601

Chain	Residue
A	GLY50
C	LYS225
C	LEU226
C	ARG227
C	GLY228
C	THR229
C	THR230
A	THR51
A	GLY52
A	LYS53
A	THR54
A	LEU55
A	GLU79
A	PHE91
A	ILE240

---

site_id	AC2
Number of Residues	15
Details	binding site for residue ADP C 601

Chain	Residue
A	LYS225
A	ARG227
A	GLY228
A	THR229
A	THR230
C	GLY50
C	THR51
C	GLY52
C	LYS53
C	THR54
C	LEU55
C	ASN87
C	SER90
C	PHE91
C	ILE240

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
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	2
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_FI3
Number of Residues	1
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_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"7DY1","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	42
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_FI6
Number of Residues	13
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01836","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
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_FI8
Number of Residues	2
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

---