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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
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0008270molecular_functionzinc ion binding
A0008703molecular_function5-amino-6-(5-phosphoribosylamino)uracil reductase activity
A0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
A0009231biological_processriboflavin biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0050661molecular_functionNADP binding
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0008270molecular_functionzinc ion binding
B0008703molecular_function5-amino-6-(5-phosphoribosylamino)uracil reductase activity
B0008835molecular_functiondiaminohydroxyphosphoribosylaminopyrimidine deaminase activity
B0009231biological_processriboflavin biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0050661molecular_functionNADP binding
Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues39
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAEvhALrmagekakgatayvtle................PCshhgrtppCcdaL
ChainResidueDetails
AHIS50-LEU88

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU52
BGLU52

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS50
ACYS75
ACYS84
BHIS50
BCYS75
BCYS84

site_idSWS_FT_FI3
Number of Residues22
DetailsBINDING:
ChainResidueDetails
ATHR161
AGLU299
AGLY301
BTHR161
BSER168
BTRP170
BARG184
BTHR196
BASP200
BLEU204
BARG207
ASER168
BSER234
BGLU299
BGLY301
ATRP170
AARG184
ATHR196
AASP200
ALEU204
AARG207
ASER234

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PDB entries from 2024-07-24

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