2PUK

Crystal structure of the binary complex between ferredoxin: thioredoxin reductase and thioredoxin m

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	0015035	molecular_function	protein-disulfide reductase activity
E	0005515	molecular_function	protein binding
E	0009055	molecular_function	electron transfer activity
E	0015979	biological_process	photosynthesis
E	0016491	molecular_function	oxidoreductase activity
E	0016730	molecular_function	oxidoreductase activity, acting on iron-sulfur proteins as donors
E	0046872	molecular_function	metal ion binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	0103012	molecular_function	ferredoxin-thioredoxin reductase activity
F	0005515	molecular_function	protein binding
F	0015979	biological_process	photosynthesis
F	0016491	molecular_function	oxidoreductase activity
G	0015035	molecular_function	protein-disulfide reductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 A 1000

Chain	Residue
A	CYS55
A	CYS74
A	CYS76
A	MET79
A	CYS85
A	HIS86
A	CYS87
A	PHE90

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 E 1000

Chain	Residue
E	CYS74
E	CYS76
E	MET79
E	CYS85
E	HIS86
E	CYS87
E	CYS55

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:10649999, ECO:0000269|PubMed:14769790, ECO:0000269|PubMed:17611542, ECO:0000269|PubMed:19132843

Chain	Residue	Details
A	CYS57
E	CYS57
G	CYS37
G	SER40

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:10649999, ECO:0000269|PubMed:17611542

Chain	Residue	Details
A	CYS55
A	CYS74
A	CYS76
A	CYS85
E	CYS55
E	CYS74
E	CYS76
E	CYS85

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Increases the nucleophilicity of the active site Cys => ECO:0000269|PubMed:19132843

Chain	Residue	Details
A	HIS86
E	HIS86
G	GLY38
G	PRO39

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1cqg

Chain	Residue	Details
C	SER40
C	CYS37

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1cqg

Chain	Residue	Details
G	SER40
G	CYS37

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