2OBC

The crystal structure of RibD from Escherichia coli in complex with a substrate analogue, ribose 5-phosphate (beta form), bound to the active site of the reductase domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005515	molecular_function	protein binding
A	0008270	molecular_function	zinc ion binding
A	0008703	molecular_function	5-amino-6-(5-phosphoribosylamino)uracil reductase activity
A	0008835	molecular_function	diaminohydroxyphosphoribosylaminopyrimidine deaminase activity
A	0009231	biological_process	riboflavin biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
A	0050661	molecular_function	NADP binding
B	0003824	molecular_function	catalytic activity
B	0005515	molecular_function	protein binding
B	0008270	molecular_function	zinc ion binding
B	0008703	molecular_function	5-amino-6-(5-phosphoribosylamino)uracil reductase activity
B	0008835	molecular_function	diaminohydroxyphosphoribosylaminopyrimidine deaminase activity
B	0009231	biological_process	riboflavin biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
B	0050661	molecular_function	NADP binding

Functional Information from PROSITE/UniProt

site_id	PS00903
Number of Residues	39
Details	CYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAEvhALrmagekakgatayvtle................PCshhgrtppCcdaL

Chain	Residue	Details
A	HIS50-LEU88

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	5
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Chain

Residue

Details