2PVG

Crystal srtucture of the binary complex between ferredoxin and ferredoxin:thioredoxin reductase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0009055	molecular_function	electron transfer activity
A	0015979	biological_process	photosynthesis
A	0016491	molecular_function	oxidoreductase activity
A	0016730	molecular_function	oxidoreductase activity, acting on iron-sulfur proteins as donors
A	0046872	molecular_function	metal ion binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	0103012	molecular_function	ferredoxin-thioredoxin reductase activity
B	0005515	molecular_function	protein binding
B	0015979	biological_process	photosynthesis
B	0016491	molecular_function	oxidoreductase activity
C	0005515	molecular_function	protein binding
C	0009055	molecular_function	electron transfer activity
C	0022900	biological_process	electron transport chain
C	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES C 300

Chain	Residue
C	SER38
C	CYS39
C	ARG40
C	GLY42
C	ALA43
C	CYS44
C	CYS47
C	LEU75
C	CYS77

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 A 400

Chain	Residue
A	VAL39
A	CYS55
A	CYS74
A	CYS76
A	MET79
A	CYS85
A	HIS86
A	CYS87
A	HOH428

---

Functional Information from PROSITE/UniProt

site_id	PS00197
Number of Residues	9
Details	2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRAGACSTC

Chain	Residue	Details
C	CYS39-CYS47

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00465, ECO:0000269|PubMed:7578051

Chain	Residue	Details
C	CYS39
C	CYS44
C	CYS47
C	CYS77

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10649999, ECO:0000269|PubMed:17611542

Chain	Residue	Details
A	CYS55
A	CYS74
A	CYS76
A	CYS85

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Increases the nucleophilicity of the active site Cys => ECO:0000269|PubMed:19132843

Chain	Residue	Details
A	HIS86

---