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	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	0006338	biological_process	chromatin remodeling
A	0006355	biological_process	regulation of DNA-templated transcription
A	0007623	biological_process	circadian rhythm
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
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	0044024	molecular_function	histone H2AS1 kinase activity
A	0046777	biological_process	protein autophosphorylation
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	0048511	biological_process	rhythmic process
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	0006338	biological_process	chromatin remodeling
C	0006355	biological_process	regulation of DNA-templated transcription
C	0007623	biological_process	circadian rhythm
C	0016301	molecular_function	kinase activity
C	0016310	biological_process	phosphorylation
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	0044024	molecular_function	histone H2AS1 kinase activity
C	0046777	biological_process	protein autophosphorylation
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	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	2
Details	ACT_SITE: Proton acceptor in CI (KaiC 1) => ECO:0000305|PubMed:35507871

Chain	Residue	Details
A	GLU78
C	GLU78

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor in CII (KaiC 2) => ECO:0000305|PubMed:35507871

Chain	Residue	Details
A	GLU318
C	GLU318

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000312|PDB:7DY1

Chain	Residue	Details
A	SER49
C	SER49

---

site_id	SWS_FT_FI4
Number of Residues	42
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000312|PDB:7DY1

Chain	Residue	Details
A	GLY50
A	HIS231
A	THR290
A	GLY291
A	THR292
A	GLY293
A	LYS294
A	THR295
A	LEU296
A	ARG451
A	LYS457
A	THR51
A	MET458
A	ARG459
C	GLY50
C	THR51
C	GLY52
C	LYS53
C	LEU55
C	SER90
C	LYS225
C	LEU226
A	GLY52
C	ARG227
C	HIS231
C	THR290
C	GLY291
C	THR292
C	GLY293
C	LYS294
C	THR295
C	LEU296
C	ARG451
A	LYS53
C	LYS457
C	MET458
C	ARG459
A	LEU55
A	SER90
A	LYS225
A	LEU226
A	ARG227

---

site_id	SWS_FT_FI5
Number of Residues	14
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836

Chain	Residue	Details
A	THR54
C	GLU318
C	TRP331
C	SER461
C	HIS463
C	LYS465
A	THR229
A	GLU318
A	TRP331
A	SER461
A	HIS463
A	LYS465
C	THR54
C	THR229

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:24112939

Chain	Residue	Details
A	GLU431
C	GLU431

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:24112939

Chain	Residue	Details
A	THR432
C	THR432

---