1SRR

CRYSTAL STRUCTURE OF A PHOSPHATASE RESISTANT MUTANT OF SPORULATION RESPONSE REGULATOR SPO0F FROM BACILLUS SUBTILIS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000160	biological_process	phosphorelay signal transduction system
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0016301	molecular_function	kinase activity
A	0030435	biological_process	sporulation resulting in formation of a cellular spore
A	0046872	molecular_function	metal ion binding
B	0000160	biological_process	phosphorelay signal transduction system
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0016301	molecular_function	kinase activity
B	0030435	biological_process	sporulation resulting in formation of a cellular spore
B	0046872	molecular_function	metal ion binding
C	0000160	biological_process	phosphorelay signal transduction system
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0016301	molecular_function	kinase activity
C	0030435	biological_process	sporulation resulting in formation of a cellular spore
C	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 531

Chain	Residue
A	ASP11
A	ASP54
A	LYS56
A	HOH646
A	HOH781

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C 532

Chain	Residue
C	ASP11
C	ASP54
C	LYS56
C	HOH788

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
A	ASP10
C	ASP11
C	ASP54
C	LYS56
A	ASP11
A	ASP54
A	LYS56
B	ASP10
B	ASP11
B	ASP54
B	LYS56
C	ASP10

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site_id	SWS_FT_FI2
Number of Residues	3
Details	MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:9254596

Chain	Residue	Details
A	ASP54
B	ASP54
C	ASP54

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