2D2A

Crystal Structure of Escherichia coli SufA Involved in Biosynthesis of Iron-sulfur Clusters

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006979	biological_process	response to oxidative stress
A	0016226	biological_process	iron-sulfur cluster assembly
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	0097428	biological_process	protein maturation by iron-sulfur cluster transfer
A	1990230	cellular_component	iron-sulfur cluster transfer complex
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006979	biological_process	response to oxidative stress
B	0016226	biological_process	iron-sulfur cluster assembly
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0097428	biological_process	protein maturation by iron-sulfur cluster transfer
B	1990230	cellular_component	iron-sulfur cluster transfer complex

Functional Information from PROSITE/UniProt

site_id	PS01152
Number of Residues	18
Details	HESB Hypothetical hesB/yadR/yfhF family signature. FkFhNPKaqneCgCGeSF

Chain	Residue	Details
A	PHE103-PHE120

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: sulfuration is probably achieved via an internal sulfur transfer from C-114 or C-116 => ECO:0000269\|PubMed:17350000