Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4TLC

Crystal structure of N-terminal C1 domain of KaiC

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
B	0005524	molecular_function	ATP binding
C	0005524	molecular_function	ATP binding
D	0005524	molecular_function	ATP binding
E	0005524	molecular_function	ATP binding
F	0005524	molecular_function	ATP binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 301

Chain	Residue
A	THR53
A	AGS303
A	HOH410
A	HOH411
A	HOH412

site_id	AC2
Number of Residues	2
Details	binding site for residue CL A 302

Chain	Residue
A	ARG218
A	ILE239

site_id	AC3
Number of Residues	31
Details	binding site for residue AGS A 303

Chain	Residue
A	THR50
A	GLY51
A	LYS52
A	THR53
A	LEU54
A	SER89
A	PHE90
A	ARG218
A	ILE239
A	THR240
A	ASP241
A	MG301
A	HOH410
A	HOH411
A	HOH412
A	HOH416
A	HOH449
A	HOH484
A	HOH495
B	PHE199
B	LYS224
B	LEU225
B	ARG226
B	THR228
B	SER229
B	HIS230
B	HOH437
B	HOH461
B	HOH470
A	SER48
A	GLY49

site_id	AC4
Number of Residues	5
Details	binding site for residue MG B 301

Chain	Residue
B	THR53
B	AGS303
B	HOH422
B	HOH423
B	HOH424

site_id	AC5
Number of Residues	4
Details	binding site for residue CL B 302

Chain	Residue
B	ARG218
B	THR238
B	ILE239
B	HOH430

site_id	AC6
Number of Residues	28
Details	binding site for residue AGS B 303

Chain	Residue
B	SER48
B	GLY49
B	THR50
B	GLY51
B	LYS52
B	THR53
B	LEU54
B	SER89
B	PHE90
B	ARG218
B	ILE239
B	ASP241
B	MG301
B	HOH410
B	HOH422
B	HOH423
B	HOH424
B	HOH425
B	HOH430
B	HOH460
B	HOH555
C	PHE199
C	LYS224
C	LEU225
C	ARG226
C	THR228
C	HIS230
C	HOH484

site_id	AC7
Number of Residues	5
Details	binding site for residue MG C 301

Chain	Residue
C	THR53
C	AGS303
C	HOH423
C	HOH424
C	HOH425

site_id	AC8
Number of Residues	4
Details	binding site for residue CL C 302

Chain	Residue
C	ARG218
C	THR238
C	ILE239
D	HOH530

site_id	AC9
Number of Residues	28
Details	binding site for residue AGS C 303

Chain	Residue
C	HOH425
C	HOH462
C	HOH502
D	PHE199
D	LYS224
D	LEU225
D	ARG226
D	THR228
D	SER229
D	HIS230
D	HOH443
D	HOH527
D	HOH530
C	SER48
C	GLY49
C	THR50
C	GLY51
C	LYS52
C	THR53
C	LEU54
C	SER89
C	PHE90
C	ARG218
C	ILE239
C	ASP241
C	MG301
C	HOH423
C	HOH424

site_id	AD1
Number of Residues	5
Details	binding site for residue MG D 301

Chain	Residue
D	THR53
D	AGS303
D	HOH424
D	HOH425
D	HOH426

site_id	AD2
Number of Residues	3
Details	binding site for residue CL D 302

Chain	Residue
D	ARG218
D	THR238
D	ILE239

site_id	AD3
Number of Residues	31
Details	binding site for residue AGS D 303

Chain	Residue
D	SER48
D	GLY49
D	THR50
D	GLY51
D	LYS52
D	THR53
D	LEU54
D	SER89
D	PHE90
D	ARG218
D	ILE239
D	THR240
D	ASP241
D	MG301
D	HOH424
D	HOH425
D	HOH426
D	HOH433
D	HOH493
D	HOH543
E	PHE199
E	LYS224
E	LEU225
E	ARG226
E	THR228
E	SER229
E	HIS230
E	LYS232
E	HOH426
E	HOH465
E	HOH497

site_id	AD4
Number of Residues	6
Details	binding site for residue MG E 301

Chain	Residue
E	THR53
E	GLU78
E	AGS303
E	HOH416
E	HOH417
E	HOH418

site_id	AD5
Number of Residues	3
Details	binding site for residue CL E 302

Chain	Residue
E	ARG218
E	THR238
E	ILE239

site_id	AD6
Number of Residues	31
Details	binding site for residue AGS E 303

Chain	Residue
E	SER48
E	GLY49
E	THR50
E	GLY51
E	LYS52
E	THR53
E	LEU54
E	SER89
E	PHE90
E	ARG218
E	ILE239
E	ASP241
E	MG301
E	HOH416
E	HOH417
E	HOH418
E	HOH424
E	HOH456
E	HOH486
E	HOH528
F	PHE199
F	LYS224
F	LEU225
F	ARG226
F	THR228
F	SER229
F	HIS230
F	LYS232
F	HOH437
F	HOH460
F	HOH508

site_id	AD7
Number of Residues	27
Details	binding site for residue AGS F 303

Chain	Residue
A	PHE199
A	LYS224
A	LEU225
A	ARG226
A	GLY227
A	THR228
A	SER229
A	HIS230
A	LYS232
A	HOH477
F	SER48
F	GLY49
F	THR50
F	GLY51
F	LYS52
F	THR53
F	LEU54
F	PHE90
F	ARG218
F	ILE239
F	ASP241
F	MG301
F	HOH426
F	HOH428
F	HOH430
F	HOH431
F	HOH434

site_id	AD8
Number of Residues	5
Details	binding site for residue MG F 301

Chain	Residue
F	THR53
F	AGS303
F	HOH426
F	HOH430
F	HOH431

site_id	AD9
Number of Residues	3
Details	binding site for residue CL F 302

Chain	Residue
F	ARG218
F	THR238
F	ILE239

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Proton acceptor in CI (KaiC 1) => ECO:0000305\|PubMed:22304631

Chain	Residue	Details
A	GLU77
B	GLU77
C	GLU77
D	GLU77
E	GLU77
F	GLU77

site_id	SWS_FT_FI2
Number of Residues	72
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
B	GLY49
B	THR50
B	GLY51
B	LYS52
B	LEU54
B	SER89
B	LYS224
A	THR50
B	ARG226
B	THR228
B	HIS230
B	THR240
B	ASP241
C	GLY49
C	THR50
C	GLY51
C	LYS52
C	LEU54
A	GLY51
C	SER89
C	LYS224
C	ARG226
C	THR228
C	HIS230
C	THR240
C	ASP241
D	GLY49
D	THR50
D	GLY51
A	LYS52
D	LYS52
D	LEU54
D	SER89
D	LYS224
D	ARG226
D	THR228
D	HIS230
D	THR240
D	ASP241
E	GLY49
A	LEU54
E	THR50
E	GLY51
E	LYS52
E	LEU54
E	SER89
E	LYS224
E	ARG226
E	THR228
E	HIS230
E	THR240
A	SER89
E	ASP241
F	GLY49
F	THR50
F	GLY51
F	LYS52
F	LEU54
F	SER89
F	LYS224
F	ARG226
F	THR228
A	LYS224
F	HIS230
F	THR240
F	ASP241
A	ARG226
A	THR228

site_id	SWS_FT_FI3
Number of Residues	6
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
C	THR53
D	THR53
E	THR53
F	THR53

site_id	SWS_FT_FI4
Number of Residues	6
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
B	LEU225
C	LEU225
D	LEU225
E	LEU225
F	LEU225

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