9OFH

Extended conformation of dusk state KaiC

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	6
Details	ACT_SITE: Proton acceptor in CII (KaiC 2) => ECO:0000305|PubMed:22304631

Chain	Residue	Details
A	GLU318
B	GLU318
C	GLU318
D	GLU318
E	GLU318
F	GLU318

---

site_id	SWS_FT_FI3
Number of Residues	150
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
D	LYS465
E	GLY49
E	THR50
E	GLY51
E	LYS52
E	LEU54
E	SER89
E	LYS224
E	ARG226
E	THR228
A	THR240
E	HIS230
E	THR240
E	ASP241
E	THR290
E	GLY291
E	THR292
E	GLY293
E	LYS294
E	LEU296
E	TRP331
A	ASP241
E	ARG451
E	LYS457
E	ARG459
E	SER461
E	HIS463
E	LYS465
F	GLY49
F	THR50
F	GLY51
F	LYS52
A	THR290
F	LEU54
F	SER89
F	LYS224
F	ARG226
F	THR228
F	HIS230
F	THR240
F	ASP241
F	THR290
F	GLY291
A	GLY291
F	THR292
F	GLY293
F	LYS294
F	LEU296
F	TRP331
F	ARG451
F	LYS457
F	ARG459
F	SER461
F	HIS463
A	THR292
F	LYS465
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
C	GLY49
C	THR50
C	GLY51
C	LYS52
C	LEU54
C	SER89
C	LYS224
C	ARG226
C	THR228
A	SER89
C	HIS230
C	THR240
C	ASP241
C	THR290
C	GLY291
C	THR292
C	GLY293
C	LYS294
C	LEU296
C	TRP331
A	LYS224
C	ARG451
C	LYS457
C	ARG459
C	SER461
C	HIS463
C	LYS465
D	GLY49
D	THR50
D	GLY51
D	LYS52
A	ARG226
D	LEU54
D	SER89
D	LYS224
D	ARG226
D	THR228
D	HIS230
D	THR240
D	ASP241
D	THR290
D	GLY291
A	THR228
D	THR292
D	GLY293
D	LYS294
D	LEU296
D	TRP331
D	ARG451
D	LYS457
D	ARG459
D	SER461
D	HIS463

---

site_id	SWS_FT_FI4
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_FI5
Number of Residues	12
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
E	MET458
F	LEU225
F	MET458
A	MET458
B	LEU225
B	MET458
C	LEU225
C	MET458
D	LEU225
D	MET458
E	LEU225

---

site_id	SWS_FT_FI6
Number of Residues	6
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
C	THR295
D	THR295
E	THR295
F	THR295

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:15304218, ECO:0000269|PubMed:16628225

Chain	Residue	Details
A	GLU318
B	GLU318
C	GLU318
D	GLU318
E	GLU318
F	GLU318

---

site_id	SWS_FT_FI8
Number of Residues	6
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	GLU431
B	GLU431
C	GLU431
D	GLU431
E	GLU431
F	GLU431

---

site_id	SWS_FT_FI9
Number of Residues	6
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	GLU432
B	GLU432
C	GLU432
D	GLU432
E	GLU432
F	GLU432

---