2E0I

Crystal structure of archaeal photolyase from Sulfolobus tokodaii with two FAD molecules: Implication of a novel light-harvesting cofactor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003677	molecular_function	DNA binding
A	0003904	molecular_function	deoxyribodipyrimidine photo-lyase activity
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006950	biological_process	response to stress
A	0016829	molecular_function	lyase activity
A	0071949	molecular_function	FAD binding
B	0000166	molecular_function	nucleotide binding
B	0003677	molecular_function	DNA binding
B	0003904	molecular_function	deoxyribodipyrimidine photo-lyase activity
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006950	biological_process	response to stress
B	0016829	molecular_function	lyase activity
B	0071949	molecular_function	FAD binding
C	0000166	molecular_function	nucleotide binding
C	0003677	molecular_function	DNA binding
C	0003904	molecular_function	deoxyribodipyrimidine photo-lyase activity
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0006950	biological_process	response to stress
C	0016829	molecular_function	lyase activity
C	0071949	molecular_function	FAD binding
D	0000166	molecular_function	nucleotide binding
D	0003677	molecular_function	DNA binding
D	0003904	molecular_function	deoxyribodipyrimidine photo-lyase activity
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0006950	biological_process	response to stress
D	0016829	molecular_function	lyase activity
D	0071949	molecular_function	FAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FAD A 1100

Chain	Residue
A	PHE202
A	ARG247
A	TYR306
A	ILE307
A	GLY309
A	ARG312
A	MET313
A	ALA316
A	LEU338
A	ASP340
A	ASP342
A	ASN213
A	ILE345
A	ASN346
A	ASN349
A	MPD3005
A	TYR214
A	ARG215
A	LEU216
A	SER217
A	LEU220
A	GLU243
A	TRP246

---

site_id	AC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE FAD A 1200

Chain	Residue
A	ARG8
A	ARG9
A	PHE33
A	ILE34
A	ALA35
A	ASP36
A	ARG38
A	GLN39
A	LEU40
A	ASN43
A	TYR45
A	VAL51
A	MET54
A	ASP98
A	THR100
A	PHE102
A	ARG106
A	LYS221
A	GLU331
A	TYR341
A	PRO343
A	MPD3001
A	HOH5027
A	HOH5053
A	HOH5121

---

site_id	AC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE FAD B 1300

Chain	Residue
B	PHE202
B	ASN213
B	TYR214
B	ARG215
B	LEU216
B	SER217
B	LEU220
B	GLU243
B	ARG247
B	TYR306
B	GLY309
B	ARG312
B	MET313
B	ALA316
B	LEU338
B	ASP340
B	TYR341
B	ASP342
B	ILE345
B	ASN346
B	ASN349

---

site_id	AC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FAD B 1400

Chain	Residue
B	ARG8
B	ARG9
B	PHE33
B	ILE34
B	ALA35
B	ASP36
B	GLN39
B	LEU40
B	ASN43
B	TYR45
B	VAL51
B	MET54
B	ASP98
B	THR100
B	PHE102
B	ARG106
B	LYS221
B	GLU331
B	TYR341
B	PRO343
B	MPD3002
B	HOH5040
B	HOH5145
B	HOH5150

---

site_id	AC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FAD C 1500

Chain	Residue
C	LEU220
C	GLU243
C	TRP246
C	ARG247
C	TYR306
C	GLY309
C	ARG312
C	PHE334
C	LEU338
C	ASP340
C	TYR341
C	ASP342
C	ILE345
C	ASN346
C	ASN349
C	MPD3006
C	PHE202
C	ASN213
C	TYR214
C	ARG215
C	LEU216
C	SER217

---

site_id	AC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE FAD C 1600

Chain	Residue
C	ARG8
C	ARG9
C	PHE33
C	ILE34
C	ALA35
C	ASP36
C	ARG38
C	GLN39
C	LEU40
C	ASN43
C	TYR45
C	VAL51
C	MET54
C	ASP98
C	THR100
C	PHE102
C	ARG106
C	LYS221
C	GLU331
C	TYR341
C	PRO343
C	MPD3003
C	HOH5021
C	HOH5032
C	HOH5097
C	HOH5131

---

site_id	AC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FAD D 1700

Chain	Residue
D	PHE202
D	ASN213
D	TYR214
D	ARG215
D	LEU216
D	SER217
D	LEU220
D	GLU243
D	TRP246
D	ARG247
D	TYR306
D	GLY309
D	ARG312
D	MET313
D	ALA316
D	LEU338
D	ASP340
D	TYR341
D	ASP342
D	ILE345
D	ASN346
D	ASN349

---

site_id	AC8
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FAD D 1800

Chain	Residue
D	ARG8
D	ARG9
D	PHE33
D	ILE34
D	ALA35
D	ASP36
D	GLN39
D	LEU40
D	ASN43
D	TYR45
D	VAL51
D	MET54
D	ASP98
D	THR100
D	PHE102
D	ARG106
D	LYS221
D	GLU331
D	TYR341
D	PRO343
D	MPD3004
D	HOH5011
D	HOH5024
D	HOH5143

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 3001

Chain	Residue
A	THR100
A	PRO101
A	PHE102
A	PHE261
A	FAD1200

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD B 3002

Chain	Residue
B	PRO101
B	PHE102
B	PHE261
B	FAD1400

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD C 3003

Chain	Residue
C	THR100
C	PRO101
C	PHE102
C	PHE261
C	FAD1600

---

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD D 3004

Chain	Residue
D	THR100
D	PRO101
D	PHE102
D	PHE261
D	FAD1800

---

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 3005

Chain	Residue
A	GLU243
A	TRP246
A	MET313
A	TRP352
A	FAD1100

---

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD C 3006

Chain	Residue
C	GLU243
C	MET313
C	TRP352
C	FAD1500

---

Functional Information from PROSITE/UniProt

site_id	PS00394
Number of Residues	13
Details	DNA_PHOTOLYASES_1_1 DNA photolyases class 1 signature 1. TGyPIIDAgMRmL

Chain	Residue	Details
A	THR289-LEU301

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1dnp

Chain	Residue	Details
A	TRP350
A	TRP274
A	TRP327

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1dnp

Chain	Residue	Details
B	TRP350
B	TRP274
B	TRP327

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1dnp

Chain	Residue	Details
C	TRP350
C	TRP274
C	TRP327

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1dnp

Chain	Residue	Details
D	TRP350
D	TRP274
D	TRP327

---