1URH

The "Rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfotransferases: Crystal structure of SseA from Escherichia coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004792	molecular_function	thiosulfate sulfurtransferase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006979	biological_process	response to oxidative stress
A	0016740	molecular_function	transferase activity
A	0016783	molecular_function	sulfurtransferase activity
A	0016784	molecular_function	3-mercaptopyruvate sulfurtransferase activity
A	0042262	biological_process	DNA protection
A	0046677	biological_process	response to antibiotic
B	0004792	molecular_function	thiosulfate sulfurtransferase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006979	biological_process	response to oxidative stress
B	0016740	molecular_function	transferase activity
B	0016783	molecular_function	sulfurtransferase activity
B	0016784	molecular_function	3-mercaptopyruvate sulfurtransferase activity
B	0042262	biological_process	DNA protection
B	0046677	biological_process	response to antibiotic

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO3 B1268

Chain	Residue
B	PHE223

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Functional Information from PROSITE/UniProt

site_id	PS00380
Number of Residues	12
Details	RHODANESE_1 Rhodanese signature 1. YlngHIPGAvfF

Chain	Residue	Details
A	TYR41-PHE52

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site_id	PS00683
Number of Residues	11
Details	RHODANESE_2 Rhodanese C-terminal signature. VklYDGAWsEW

Chain	Residue	Details
A	VAL258-TRP268

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Cysteine persulfide intermediate

Chain	Residue	Details
A	GLY238
B	GLY238

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	PHE179
B	PHE179

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