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	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
A	0051604	biological_process	protein maturation
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	0051536	molecular_function	iron-sulfur cluster binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0051604	biological_process	protein maturation

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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Binding site: {"description":"sulfuration is probably achieved via an internal sulfur transfer from C-114 or C-116","evidences":[{"source":"PubMed","id":"17350000","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17350000","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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