6X24

Structural basis of plant blue light photoreceptor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0009785	biological_process	blue light signaling pathway
A	0009882	molecular_function	blue light photoreceptor activity
B	0009785	biological_process	blue light signaling pathway
B	0009882	molecular_function	blue light photoreceptor activity
C	0009785	biological_process	blue light signaling pathway
C	0009882	molecular_function	blue light photoreceptor activity
D	0009785	biological_process	blue light signaling pathway
D	0009882	molecular_function	blue light photoreceptor activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue FAD A 501

Chain	Residue
A	TYR232
A	LEU293
A	ARG294
A	TRP353
A	ASN356
A	ARG359
A	LEU385
A	ASP387
A	ALA388
A	ASP389
A	CYS392
A	THR244
A	ASP393
A	GLY396
A	SER245
A	LEU246
A	LEU247
A	SER248
A	LEU251
A	GLY290
A	ILE291

---

site_id	AC2
Number of Residues	5
Details	binding site for residue GOL A 502

Chain	Residue
A	GLY464
A	THR465
A	ASN466
A	TYR467
A	ALA468

---

site_id	AC3
Number of Residues	3
Details	binding site for residue GOL A 503

Chain	Residue
A	ARG13
A	ILE37
A	GLU43

---

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 504

Chain	Residue
A	ARG332
A	GLN333
A	TRP349
A	TYR380
B	GLY460

---

site_id	AC5
Number of Residues	2
Details	binding site for residue GOL A 505

Chain	Residue
A	ARG266
D	PRO171

---

site_id	AC6
Number of Residues	21
Details	binding site for residue FAD B 501

Chain	Residue
B	TYR232
B	THR244
B	SER245
B	LEU246
B	LEU247
B	SER248
B	LEU251
B	PHE287
B	GLY290
B	ILE291
B	LEU293
B	ARG294
B	TRP353
B	ASN356
B	ARG359
B	ASP387
B	ASP389
B	CYS392
B	ASP393
B	GLY396
B	GOL503

---

site_id	AC7
Number of Residues	5
Details	binding site for residue GOL B 502

Chain	Residue
B	ARG12
B	ARG13
B	PHE36
B	ILE37
B	GLU43

---

site_id	AC8
Number of Residues	4
Details	binding site for residue GOL B 503

Chain	Residue
B	TYR232
B	LEU286
B	ARG357
B	FAD501

---

site_id	AC9
Number of Residues	23
Details	binding site for residue FAD C 501

Chain	Residue
C	TYR232
C	THR244
C	SER245
C	LEU246
C	LEU247
C	SER248
C	LEU251
C	PHE287
C	GLY290
C	ILE291
C	LEU293
C	ARG294
C	TRP353
C	MET354
C	HIS355
C	ASN356
C	ARG359
C	VAL360
C	ASP387
C	ASP389
C	CYS392
C	GLY396
C	GOL505

---

site_id	AD1
Number of Residues	4
Details	binding site for residue GOL C 502

Chain	Residue
C	THR465
C	ASN466
D	THR465
D	ASN466

---

site_id	AD2
Number of Residues	2
Details	binding site for residue GOL C 503

Chain	Residue
B	CYS264
C	HIS260

---

site_id	AD3
Number of Residues	1
Details	binding site for residue GOL C 505

Chain	Residue
C	FAD501

---

site_id	AD4
Number of Residues	1
Details	binding site for residue GOL C 506

Chain	Residue
C	LYS379

---

site_id	AD5
Number of Residues	4
Details	binding site for residue GOL C 507

Chain	Residue
C	SER108
C	ARG111
C	ARG12
C	ILE37

---

site_id	AD6
Number of Residues	20
Details	binding site for residue FAD D 501

Chain	Residue
D	TYR232
D	THR244
D	SER245
D	LEU246
D	LEU247
D	SER248
D	GLY290
D	ILE291
D	LEU293
D	ARG294
D	TRP353
D	ASN356
D	ARG359
D	VAL360
D	SER363
D	ASP387
D	ASP389
D	CYS392
D	ASP393
D	GLY396

---

site_id	AD7
Number of Residues	2
Details	binding site for residue GOL D 502

Chain	Residue
C	LYS457
D	GLU199

---

site_id	AD8
Number of Residues	1
Details	binding site for residue GOL D 503

Chain	Residue
D	GLU428

---

site_id	AD9
Number of Residues	7
Details	binding site for residue GOL D 504

Chain	Residue
D	ARG12
D	ILE37
D	TRP38
D	GLU43
D	LEU103
D	SER108
D	ARG111

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	THR336-LEU348

---

site_id	PS00691
Number of Residues	20
Details	DNA_PHOTOLYASES_1_2 DNA photolyases class 1 signature 2. NRiRVIvSSFAvKfLllpWK

Chain	Residue	Details
A	ASN356-LYS375

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	516
Details	Domain: {"description":"Photolyase/cryptochrome alpha/beta","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32398826","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6K8I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6K8K","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q43125","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32398826","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6K8K","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	Site: {"description":"Involved in electron transfer from the protein surface to the FAD cofactor","evidences":[{"source":"PubMed","id":"25428980","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---